1HR7: Mitochondrial processing peptidase alpha subunit
Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant. Determined by X-ray diffraction at 2.55 Å resolution. Released 11 Jul 2001.
- Method
- X-ray diffraction
- Resolution
- 2.55 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 8
- Atoms
- 27,725
- Mol. weight
- 405.97 kDa
- Ligands
- ZN
- Released
- 11 Jul 2001
Explore 1HR7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1HR7 contains 209 α-helices and 124 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 28 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 1 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 40-46 | 7 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 60-66 | 7 | |
| β-strand | 72 | 1 | 2 |
| α-helix | 77-86 | 10 | |
| β-strand | 91-95 | 5 | 1 |
| β-strand | 100-106 | 7 | 1 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-123 | 13 | |
| β-strand | 125 | 1 | 2 |
| α-helix | 129-146 | 18 | |
| α-helix | 150-162 | 13 | |
| α-helix | 167-169 | 3 | |
| α-helix | 174-175 | 2 | |
| α-helix | 176-181 | 6 | |
| α-helix | 184-194 | 11 | |
| α-helix | 197-199 | 3 | |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 209-220 | 12 | |
| α-helix | 233-235 | 3 | |
| β-strand | 240-244 | 5 | 3 |
| α-helix | 245-248 | 4 | |
| α-helix | 254-255 | 2 | |
| β-strand | 257-264 | 8 | 3 |
| α-helix | 273-283 | 11 | |
| β-strand | 285-287 | 3 | 3 |
| α-helix | 301-302 | 2 | |
| α-helix | 303-307 | 5 | |
| β-strand | 313-322 | 10 | 3 |
| β-strand | 327-335 | 9 | 3 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-352 | 13 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-381 | 18 | |
| α-helix | 385-399 | 15 | |
| α-helix | 405-413 | 9 | |
| α-helix | 417-428 | 12 | |
| β-strand | 443-447 | 5 | 3 |
| α-helix | 450-453 | 4 | |
| α-helix | 456-462 | 7 | |
Chain B: 25 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 27-30 | 4 | 4 |
| β-strand | 36-41 | 6 | 4 |
| β-strand | 47-55 | 9 | 4 |
| α-helix | 58-60 | 3 | |
| α-helix | 68-75 | 8 | |
| β-strand | 79 | 1 | 5 |
| β-strand | 80 | 1 | 6 |
| β-strand | 84 | 1 | 5 |
| α-helix | 85-95 | 11 | |
| β-strand | 98-103 | 6 | 4 |
| β-strand | 107-115 | 9 | 4 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-131 | 13 | |
| β-strand | 133 | 1 | 6 |
| α-helix | 137-154 | 18 | |
| α-helix | 158-170 | 13 | |
| α-helix | 175-177 | 3 | |
| α-helix | 184-189 | 6 | |
| α-helix | 192-202 | 11 | |
| α-helix | 205-207 | 3 | |
| β-strand | 208-214 | 7 | 4 |
| α-helix | 218-229 | 12 | |
| α-helix | 233-235 | 3 | |
| α-helix | 248-249 | 2 | |
| β-strand | 254-259 | 6 | 7 |
| β-strand | 265-273 | 9 | 7 |
| α-helix | 282-292 | 11 | |
| β-strand | 294-296 | 3 | 7 |
| β-strand | 300 | 1 | 7 |
| α-helix | 308-314 | 7 | |
| β-strand | 322-329 | 8 | 7 |
| β-strand | 334-343 | 10 | 7 |
| α-helix | 349-364 | 16 | |
| α-helix | 370-381 | 12 | |
| α-helix | 382-386 | 5 | |
| α-helix | 391-405 | 15 | |
| α-helix | 411-419 | 9 | |
| α-helix | 423-433 | 11 | |
| β-strand | 439-445 | 7 | 7 |
| α-helix | 447-449 | 3 | |
| α-helix | 450-452 | 3 | |
| α-helix | 453-461 | 9 | |
Chain C: 27 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 8 |
| β-strand | 29-33 | 5 | 8 |
| β-strand | 40-46 | 7 | 8 |
| α-helix | 50-52 | 3 | |
| α-helix | 60-66 | 7 | |
| β-strand | 72 | 1 | 9 |
| α-helix | 77-86 | 10 | |
| β-strand | 91-95 | 5 | 8 |
| β-strand | 100-106 | 7 | 8 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-123 | 13 | |
| β-strand | 125 | 1 | 9 |
| α-helix | 129-146 | 18 | |
| α-helix | 150-162 | 13 | |
| α-helix | 167-169 | 3 | |
| α-helix | 176-181 | 6 | |
| α-helix | 184-194 | 11 | |
| α-helix | 197-199 | 3 | |
| β-strand | 200-205 | 6 | 8 |
| α-helix | 209-220 | 12 | |
| α-helix | 233-235 | 3 | |
| β-strand | 240-244 | 5 | 10 |
| α-helix | 245-248 | 4 | |
| α-helix | 254-255 | 2 | |
| β-strand | 257-264 | 8 | 10 |
| α-helix | 273-283 | 11 | |
| β-strand | 285-286 | 2 | 10 |
| α-helix | 301 | 1 | |
| α-helix | 302-307 | 6 | |
| β-strand | 313-322 | 10 | 10 |
| β-strand | 327-335 | 9 | 10 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-352 | 13 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-381 | 18 | |
| α-helix | 385-399 | 15 | |
| α-helix | 405-413 | 9 | |
| α-helix | 417-428 | 12 | |
| β-strand | 443-447 | 5 | 10 |
| α-helix | 450-453 | 4 | |
| α-helix | 456-462 | 7 | |
Chains D and F: 24 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 27-30 | 4 | 11 |
| β-strand | 36-41 | 6 | 11 |
| β-strand | 47-55 | 9 | 11 |
| α-helix | 58-60 | 3 | |
| α-helix | 68-75 | 8 | |
| β-strand | 79 | 1 | 12 |
| β-strand | 80 | 1 | 13 |
| β-strand | 84 | 1 | 12 |
| α-helix | 85-95 | 11 | |
| β-strand | 98-103 | 6 | 11 |
| β-strand | 107-115 | 9 | 11 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-131 | 13 | |
| β-strand | 133 | 1 | 13 |
| α-helix | 137-154 | 18 | |
| α-helix | 158-170 | 13 | |
| α-helix | 175-177 | 3 | |
| α-helix | 184-189 | 6 | |
| α-helix | 192-202 | 11 | |
| α-helix | 205-207 | 3 | |
| β-strand | 208-214 | 7 | 11 |
| α-helix | 218-229 | 12 | |
| α-helix | 233-235 | 3 | |
| α-helix | 248-249 | 2 | |
| β-strand | 254-259 | 6 | 14 |
| β-strand | 265-273 | 9 | 14 |
| α-helix | 282-292 | 11 | |
| β-strand | 294-296 | 3 | 14 |
| β-strand | 300 | 1 | 14 |
| α-helix | 308-314 | 7 | |
| β-strand | 322-329 | 8 | 14 |
| β-strand | 334-343 | 10 | 14 |
| α-helix | 349-364 | 16 | |
| α-helix | 370-385 | 16 | |
| α-helix | 391-405 | 15 | |
| α-helix | 411-419 | 9 | |
| α-helix | 423-433 | 11 | |
| β-strand | 439-445 | 7 | 14 |
| α-helix | 447-449 | 3 | |
| α-helix | 450-452 | 3 | |
| α-helix | 453-461 | 9 | |
Chain E: 29 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 15 |
| β-strand | 29-33 | 5 | 15 |
| β-strand | 40-46 | 7 | 15 |
| α-helix | 50-52 | 3 | |
| α-helix | 60-66 | 7 | |
| β-strand | 72 | 1 | 16 |
| α-helix | 77-86 | 10 | |
| β-strand | 91-95 | 5 | 15 |
| β-strand | 100-106 | 7 | 15 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-123 | 13 | |
| β-strand | 125 | 1 | 16 |
| α-helix | 129-146 | 18 | |
| α-helix | 150-162 | 13 | |
| α-helix | 167-169 | 3 | |
| α-helix | 174-175 | 2 | |
| α-helix | 176-181 | 6 | |
| α-helix | 184-194 | 11 | |
| α-helix | 197-199 | 3 | |
| β-strand | 200-205 | 6 | 15 |
| α-helix | 209-220 | 12 | |
| α-helix | 228-230 | 3 | |
| α-helix | 233-235 | 3 | |
| β-strand | 240-244 | 5 | 17 |
| α-helix | 245-248 | 4 | |
| α-helix | 254-255 | 2 | |
| β-strand | 257-264 | 8 | 17 |
| α-helix | 273-283 | 11 | |
| β-strand | 285-287 | 3 | 17 |
| α-helix | 301 | 1 | |
| α-helix | 302-307 | 6 | |
| β-strand | 313-322 | 10 | 17 |
| β-strand | 327-335 | 9 | 17 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-352 | 13 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-381 | 18 | |
| α-helix | 385-399 | 15 | |
| α-helix | 405-413 | 9 | |
| α-helix | 417-428 | 12 | |
| β-strand | 443-447 | 5 | 17 |
| α-helix | 450-453 | 4 | |
| α-helix | 456-462 | 7 | |
Chain G: 28 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 22 |
| β-strand | 29-33 | 5 | 22 |
| β-strand | 40-46 | 7 | 22 |
| α-helix | 50-52 | 3 | |
| α-helix | 60-66 | 7 | |
| β-strand | 72 | 1 | 23 |
| α-helix | 77-86 | 10 | |
| β-strand | 91-95 | 5 | 22 |
| β-strand | 100-106 | 7 | 22 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-123 | 13 | |
| β-strand | 125 | 1 | 23 |
| α-helix | 129-146 | 18 | |
| α-helix | 150-162 | 13 | |
| α-helix | 167-169 | 3 | |
| α-helix | 174-175 | 2 | |
| α-helix | 176-181 | 6 | |
| α-helix | 184-194 | 11 | |
| α-helix | 197-199 | 3 | |
| β-strand | 200-205 | 6 | 22 |
| α-helix | 209-220 | 12 | |
| α-helix | 233-235 | 3 | |
| β-strand | 240-244 | 5 | 24 |
| α-helix | 245-248 | 4 | |
| α-helix | 254-255 | 2 | |
| β-strand | 257-264 | 8 | 24 |
| α-helix | 273-283 | 11 | |
| β-strand | 285-286 | 2 | 24 |
| α-helix | 301 | 1 | |
| α-helix | 302-307 | 6 | |
| β-strand | 313-322 | 10 | 24 |
| β-strand | 327-335 | 9 | 24 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-352 | 13 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-381 | 18 | |
| α-helix | 385-399 | 15 | |
| α-helix | 405-413 | 9 | |
| α-helix | 417-428 | 12 | |
| β-strand | 443-447 | 5 | 24 |
| α-helix | 450-453 | 4 | |
| α-helix | 456-461 | 6 | |
Chain H: 24 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 27-30 | 4 | 25 |
| β-strand | 36-41 | 6 | 25 |
| β-strand | 47-55 | 9 | 25 |
| α-helix | 57-60 | 4 | |
| α-helix | 68-75 | 8 | |
| β-strand | 79 | 1 | 26 |
| β-strand | 80 | 1 | 27 |
| β-strand | 84 | 1 | 26 |
| α-helix | 85-95 | 11 | |
| β-strand | 98-103 | 6 | 25 |
| β-strand | 107-115 | 9 | 25 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-131 | 13 | |
| β-strand | 133 | 1 | 27 |
| α-helix | 137-154 | 18 | |
| α-helix | 158-170 | 13 | |
| α-helix | 175-177 | 3 | |
| α-helix | 184-189 | 6 | |
| α-helix | 192-202 | 11 | |
| α-helix | 205-207 | 3 | |
| β-strand | 208-214 | 7 | 25 |
| α-helix | 218-229 | 12 | |
| α-helix | 233-235 | 3 | |
| α-helix | 248-249 | 2 | |
| β-strand | 254-259 | 6 | 28 |
| β-strand | 265-273 | 9 | 28 |
| α-helix | 282-292 | 11 | |
| β-strand | 294-296 | 3 | 28 |
| β-strand | 300 | 1 | 28 |
| α-helix | 308-314 | 7 | |
| β-strand | 322-329 | 8 | 28 |
| β-strand | 334-343 | 10 | 28 |
| α-helix | 349-364 | 16 | |
| α-helix | 370-385 | 16 | |
| α-helix | 391-405 | 15 | |
| α-helix | 411-419 | 9 | |
| α-helix | 423-433 | 11 | |
| β-strand | 439-445 | 7 | 28 |
| α-helix | 447-449 | 3 | |
| α-helix | 450-452 | 3 | |
| α-helix | 453-461 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Mitochondrial processing peptidase alpha subunit | A, C, E, G | protein | 475 | Saccharomyces cerevisiae | P11914 (AlphaFold model) |
| Mitochondrial processing peptidase beta subunit | B, D, F, H | protein | 443 | Saccharomyces cerevisiae | P10507 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>1HR7_1 MITOCHONDRIAL PROCESSING PEPTIDASE ALPHA SUBUNIT (chains A, C, E, G)
ARTDNFKLSSLANGLKVATSNTPGHFSALGLYIDAGSRFEGRNLKGCTHILDRLAFKSTE
HVEGRAMAETLELLGGNYQCTSSRENLMYQASVFNQDVGKMLQLMSETVRFPKITEQELQ
EQKLSAEYEIDEVWMKPELVLPELLHTAAYSGETLGSPLICPRGLIPSISKYYLLDYRNK
FYTPENTVAAFVGVPHEKALELTGKYLGDWQSTHPPITKKVAQYTGGESCIPPAPVFGNL
PELFHIQIGFEGLPIDHPDIYALATLQTLLGGGGSFSAGGPGKGMYSRLYTHVLNQYYFV
ENCVAFNHSYSDSGIFGISLSCIPQAAPQAVEVIAQQMYNTFANKDLRLTEDEVSRAKNQ
LKSSLLMNLESKLVELEDMGRQVLMHGRKIPVNEMISKIEDLKPDDISRVAEMIFTGNVN
NAGNGKGRATVVMQGDRGSFGDVENVLKAYGLGNSSSSKNDSPKKKGWFHHHHHH
Sequence of entity 2 (B, D, F, H), FASTA
>1HR7_2 MITOCHONDRIAL PROCESSING PEPTIDASE BETA SUBUNIT (chains B, D, F, H)
ASQIPGTRTSKLPNGLTIATEYIPNTSSATVGIFVDAGSRAENVKNNGTAHFLQHLAFKG
TQNRPQQGIELEIENIGSHLNAYTSRENTVYYAKSLQEDIPKAVDILSDILTKSVLDNSA
IERERDVIIRESEEVDKMYDEVVFDHLHEITYKDQPLGRTILGPIKNIKSITRTDLKDYI
TKNYKGDRMVLAGAGAVDHEKLVQYAQKYFGHVPKSESPVPLGSPRGPLPVFCRGERFIK
ENTLPTTHIAIALEGVSWSAPDYFVALATQAIVGNWDRAIGTGTNSPSPLAVAASQNGSL
ANSYMSFSTSYADSGLWGMYIVTDSNEHNVRLIVNEILKEWKRIKSGKISDAEVNRAKAQ
LKAALLLSLDGSTAIVEDIGRQVVTTGKRLSPEEVFEQVDKITKDDIIMWANYRLQNKPV
SMVALGNTSTVPNVSYIEEKLNQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 4 |
Primary citation
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Taylor, A.B., Smith, B.S., Kitada, S. et al. Structure (2001) 9:615-625. DOI 10.1016/S0969-2126(01)00621-9 · PubMed
Other PDB entries of the same protein (UniProt P11914 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1HR6 2.5 Å, Yeast Mitochondrial Processing Peptidase
- 1HR8 2.7 Å, Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Cytochrome C…
- 1HR9 3.01 Å, Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate…
Browse structure collections
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