5WLW: Cysteine desulfurase, mitochondrial
Crystal Structure of the Human Mitochondrial Cysteine Desulfurase with active Cysteine Loop within ISCU1 active site, coordinating Zn ion. Complexed with human ISD11 and E. coli ACP1 at 3.3A. Determined by X-ray diffraction at 3.32 Å resolution. Released 15 Nov 2017.
- Method
- X-ray diffraction
- Resolution
- 3.32 Å
- Organisms
- Homo sapiens, Escherichia coli O45:K1 (strain S88 / ExPEC)
- Chains
- 8
- Atoms
- 9,865
- Mol. weight
- 163.1 kDa
- Ligands
- PLP, 8Q1, ZN
- Released
- 15 Nov 2017
Explore 5WLW in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5WLW contains 75 α-helices and 59 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: 21 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 56 | 1 | |
| β-strand | 57 | 1 | 1 |
| α-helix | 58 | 1 | |
| β-strand | 59-60 | 2 | 2 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-82 | 12 | |
| α-helix | 94-114 | 21 | |
| α-helix | 118-120 | 3 | |
| β-strand | 121-124 | 4 | 3 |
| α-helix | 127-132 | 6 | |
| α-helix | 133-137 | 5 | |
| α-helix | 138-141 | 4 | |
| β-strand | 148-152 | 5 | 3 |
| α-helix | 157-168 | 12 | |
| β-strand | 172-176 | 5 | 3 |
| β-strand | 178 | 1 | 4 |
| β-strand | 184 | 1 | 4 |
| α-helix | 186-192 | 7 | |
| β-strand | 197-201 | 5 | 3 |
| β-strand | 205 | 1 | 5 |
| β-strand | 211 | 1 | 6 |
| β-strand | 212 | 1 | 5 |
| α-helix | 213 | 1 | |
| α-helix | 215-224 | 10 | |
| β-strand | 228-232 | 5 | 3 |
| β-strand | 251-255 | 5 | 3 |
| α-helix | 256-258 | 3 | |
| β-strand | 266-270 | 5 | 3 |
| α-helix | 298-334 | 37 | |
| β-strand | 340-342 | 3 | 7 |
| β-strand | 349 | 1 | 6 |
| β-strand | 353-358 | 6 | 7 |
| α-helix | 363-369 | 7 | |
| β-strand | 373-374 | 2 | 2 |
| β-strand | 376-377 | 2 | 7 |
| α-helix | 380-382 | 3 | |
| α-helix | 390-394 | 5 | |
| α-helix | 399-402 | 4 | |
| β-strand | 405-409 | 5 | 7 |
| α-helix | 416-435 | 20 | |
| α-helix | 438-445 | 8 | |
Chain B: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-20 | 14 | |
| α-helix | 26-42 | 17 | |
| α-helix | 49-75 | 27 | |
| α-helix | 79-80 | 2 | |
| β-strand | 81 | 1 | 1 |
Chain C: 6 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-15 | 9 | |
| α-helix | 19-21 | 3 | |
| β-strand | 27 | 1 | 8 |
| α-helix | 28-32 | 5 | |
| α-helix | 36-50 | 15 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 8 |
| α-helix | 65-71 | 7 | |
Chain D: 7 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-19 | 8 | |
| β-strand | 24 | 1 | 9 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 9 |
| β-strand | 47-54 | 8 | 9 |
| β-strand | 59 | 1 | 10 |
| β-strand | 60-68 | 9 | 9 |
| α-helix | 71-83 | 13 | |
| β-strand | 88 | 1 | 10 |
| α-helix | 91-94 | 4 | |
| α-helix | 97-104 | 8 | |
| α-helix | 108-110 | 3 | |
| α-helix | 111-130 | 20 | |
Chain E: 22 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 56 | 1 | |
| β-strand | 57 | 1 | 11 |
| α-helix | 58 | 1 | |
| β-strand | 59-60 | 2 | 12 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-82 | 12 | |
| α-helix | 94-114 | 21 | |
| α-helix | 118-120 | 3 | |
| β-strand | 121-124 | 4 | 13 |
| α-helix | 127-132 | 6 | |
| α-helix | 133-137 | 5 | |
| α-helix | 138-141 | 4 | |
| β-strand | 148-152 | 5 | 13 |
| α-helix | 157-168 | 12 | |
| β-strand | 172-176 | 5 | 13 |
| β-strand | 178 | 1 | 14 |
| α-helix | 183 | 1 | |
| β-strand | 184 | 1 | 14 |
| α-helix | 185 | 1 | |
| α-helix | 186-192 | 7 | |
| β-strand | 197-201 | 5 | 13 |
| β-strand | 205 | 1 | 15 |
| β-strand | 211 | 1 | 16 |
| β-strand | 212 | 1 | 15 |
| α-helix | 213 | 1 | |
| α-helix | 215-224 | 10 | |
| β-strand | 228-232 | 5 | 13 |
| β-strand | 251-255 | 5 | 13 |
| α-helix | 256-258 | 3 | |
| β-strand | 266-270 | 5 | 13 |
| α-helix | 298-334 | 37 | |
| β-strand | 340-343 | 4 | 17 |
| β-strand | 349 | 1 | 16 |
| β-strand | 353-358 | 6 | 17 |
| α-helix | 363-369 | 7 | |
| β-strand | 373-374 | 2 | 12 |
| β-strand | 376-377 | 2 | 17 |
| α-helix | 390-394 | 5 | |
| α-helix | 399-402 | 4 | |
| β-strand | 405-409 | 5 | 17 |
| α-helix | 416-435 | 20 | |
| α-helix | 438-445 | 8 | |
| β-strand | 452 | 1 | 18 |
Chain F: 4 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-20 | 15 | |
| α-helix | 26-42 | 17 | |
| α-helix | 49-75 | 27 | |
| α-helix | 79-80 | 2 | |
| β-strand | 81 | 1 | 11 |
Chain G: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-15 | 9 | |
| α-helix | 19-21 | 3 | |
| β-strand | 27 | 1 | 19 |
| α-helix | 36-49 | 14 | |
| α-helix | 56-59 | 4 | |
| β-strand | 64 | 1 | 19 |
| α-helix | 65-71 | 7 | |
Chain H: 6 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-16 | 5 | |
| β-strand | 24 | 1 | 18 |
| β-strand | 34-40 | 7 | 18 |
| β-strand | 47-54 | 8 | 18 |
| β-strand | 59 | 1 | 20 |
| β-strand | 60-68 | 9 | 18 |
| α-helix | 71-83 | 13 | |
| β-strand | 88 | 1 | 20 |
| α-helix | 91-94 | 4 | |
| α-helix | 97-104 | 8 | |
| α-helix | 108-110 | 3 | |
| α-helix | 111-131 | 21 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Cysteine desulfurase, mitochondrial | A, E | protein | 406 | Homo sapiens | Q9Y697 (AlphaFold model) |
| LYR motif-containing protein 4 | B, F | protein | 91 | Homo sapiens | Q9HD34 (AlphaFold model) |
| Acyl carrier protein | C, G | protein | 77 | Escherichia coli O45:K1 (strain S88 / ExPEC) | P0A6A8 (AlphaFold model) |
| Iron-sulfur cluster assembly enzyme ISCU, mitochondrial | D, H | protein | 150 | Homo sapiens | Q9H1K1 (AlphaFold model) |
Sequence of entity 1 (A, E), FASTA
>5WLW_1 Cysteine desulfurase, mitochondrial (chains A, E)
MGSSLRPLYMDVQATTPLDPRVLDAMLPYLINYYGNPHSRTHAYGWESEAAMERARQQVA
SLIGADPREIIFTSGATESNNIAIKGVARFYRSRKKHLITTQTEHKCVLDSCRSLEAEGF
QVTYLPVQKSGIIDLKELEAAIQPDTSLVSVMTVNNEIGVKQPIAEIGRICSSRKVYFHT
DAAQAVGKIPLDVNDMKIDLMSISGHKIYGPKGVGAIYIRRRPRVRVEALQSGGGQERGM
RSGTVPTPLVVGLGAACEVAQQEMEYDHKRISKLSERLIQNIMKSLPDVVMNGDPKHHYP
GCINLSFAYVEGESLLMALKDVALSSGSACTSASLEPSYVLRAIGTDEDLAHSSIRFGIG
RFTTEEEVDYTVEKCIQHVKRLREMSPLWEMVQDGIDLKSIKWTQH
Sequence of entity 2 (B, F), FASTA
>5WLW_2 LYR motif-containing protein 4 (chains B, F)
MAASSRAQVLALYRAMLRESKRFSAYNYRTYAVRRIRDAFRENKNVKDPVEIQTLVNKAK
RDLGVIRRQVHIGQLYSTDKLIIENRDMPRT
Sequence of entity 3 (C, G), FASTA
>5WLW_3 Acyl carrier protein (chains C, G)
STIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAE
KITTVQAAIDYINGHQA
Sequence of entity 4 (D, H), FASTA
>5WLW_4 Iron-sulfur cluster assembly enzyme ISCU, mitochondrial (chains D, H)
MVLIDMSVDLSTQVVDHYENPRNVGSLDKTSKNVGTGLVGAPACGDVMKLQIQVDEKGKI
VDARFKTFGCGSAIASSSLATEWVKGKTVEEALTIKNTDIAKELCLPPVKLHCSILAEDA
IKAALADYKLKQEPKKGEAEKKELHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PLP | Pyridoxal-5'-phosphate | C8 H10 N O6 P | 2 |
| 8Q1 | S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}ami… | C23 H45 N2 O8 P S | 2 |
| ZN | Zinc ion | Zn | 2 |
Primary citation
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex. Boniecki, M.T., Freibert, S.A., Muhlenhoff, U. et al. Nat Commun (2017) 8:1287-1287. DOI 10.1038/s41467-017-01497-1 · PubMed
Other PDB entries of the same protein (UniProt Q9Y697 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6UXE 1.57 Å, Structure of the human mitochondrial desulfurase complex Nfs1-ISCU2(M140I)-ISD11 with…
- 6W1D 1.79 Å, Structure of human mitochondrial complex Nfs1-ISCU2 (WT)-ISD11 with E.coli ACP1 at 1.8 A…
- 6WIH 1.9 Å, N-terminal mutation of ISCU2 (L35H36) traps Nfs1 Cys loop in the active site of ISCU2…
- 6WI2 1.95 Å, Structure of human mitochondrial complex Nfs1-ISCU2-ISD11 with E.coli ACP1 at 1.95 A…
- 8TVT 2.0 Å, Structure of human Cysteine desulfurase Nfs1 with L-propargylglycine bound to active…
- 8RMC 2.26 Å, Structure of the FDX2-bound core ISC complex (proximal conformation)
- 8RMF 2.33 Å, Structure of the core ISC complex under turnover conditions (FDX2-bound in proximal…
- 8RMG 2.46 Å, Structure of the core ISC complex under turnover conditions (FDX2-bound in distal…
- 8PK8 2.49 Å, Structure of the human mitochondrial iron-sulfur cluster biosynthesis complex during…
- 8RME 2.49 Å, Structure of the core ISC complex under turnover conditions (frataxin-bound)
- 7RTK 2.5 Å, Structure of the (NIAU)2 complex with N-terminal mutation of ISCU2 Y35D at 2.5 A…
- 8RMD 2.52 Å, Structure of the FDX2-bound core ISC complex (distal conformation)
Browse structure collections
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