Structure of the Ssz1 ATPase bound to ATP and Magnesium. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Dec 2012.
Explore 4GNI in 3D Show helices and sheets RCSB PDB PDBe
4GNI contains 41 α-helices and 38 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-20 | 6 | 1 |
| β-strand | 24-31 | 8 | 1 |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 39 | 1 | |
| β-strand | 47-48 | 2 | 1 |
| β-strand | 50-54 | 5 | 2 |
| β-strand | 57-60 | 4 | 2 |
| α-helix | 61-70 | 10 | |
| α-helix | 72-74 | 3 | |
| β-strand | 75-77 | 3 | 2 |
| α-helix | 80-82 | 3 | |
| α-helix | 87-89 | 3 | |
| α-helix | 93-95 | 3 | |
| α-helix | 99-101 | 3 | |
| β-strand | 102-104 | 3 | 3 |
| β-strand | 107-112 | 6 | 3 |
| α-helix | 120-122 | 3 | |
| β-strand | 123-126 | 4 | 3 |
| α-helix | 127-146 | 20 | |
| β-strand | 152-157 | 6 | 1 |
| α-helix | 163-175 | 13 | |
| β-strand | 179-185 | 7 | 1 |
| α-helix | 186-193 | 8 | |
| β-strand | 205-212 | 8 | 4 |
| β-strand | 217-225 | 9 | 4 |
| β-strand | 228-237 | 10 | 4 |
| α-helix | 242-260 | 19 | |
| α-helix | 264-266 | 3 | |
| α-helix | 267-269 | 3 | |
| α-helix | 271-290 | 20 | |
| β-strand | 293-302 | 10 | 5 |
| β-strand | 305-312 | 8 | 5 |
| α-helix | 313-319 | 7 | |
| α-helix | 321-337 | 17 | |
| α-helix | 342-344 | 3 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 353-356 | 4 | |
| α-helix | 358-367 | 10 | |
| β-strand | 373-375 | 3 | 4 |
| α-helix | 389-402 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-20 | 6 | 6 |
| β-strand | 24-31 | 8 | 6 |
| β-strand | 34-38 | 5 | 6 |
| α-helix | 39 | 1 | |
| β-strand | 47-48 | 2 | 6 |
| β-strand | 51-54 | 4 | 7 |
| β-strand | 57-60 | 4 | 7 |
| α-helix | 61-65 | 5 | |
| α-helix | 72-74 | 3 | |
| β-strand | 75-76 | 2 | 7 |
| α-helix | 80-82 | 3 | |
| α-helix | 87-89 | 3 | |
| α-helix | 93-95 | 3 | |
| α-helix | 99-101 | 3 | |
| β-strand | 102-104 | 3 | 8 |
| β-strand | 107-112 | 6 | 8 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-126 | 4 | 8 |
| α-helix | 127-146 | 20 | |
| β-strand | 152-157 | 6 | 6 |
| α-helix | 163-175 | 13 | |
| β-strand | 179-185 | 7 | 6 |
| α-helix | 186-194 | 9 | |
| β-strand | 205-212 | 8 | 9 |
| β-strand | 217-225 | 9 | 9 |
| β-strand | 228-237 | 10 | 9 |
| α-helix | 242-260 | 19 | |
| α-helix | 264-266 | 3 | |
| α-helix | 267-269 | 3 | |
| α-helix | 271-287 | 17 | |
| β-strand | 293-302 | 10 | 10 |
| β-strand | 305-312 | 8 | 10 |
| α-helix | 313-337 | 25 | |
| α-helix | 342-344 | 3 | |
| β-strand | 347-351 | 5 | 9 |
| α-helix | 353-356 | 4 | |
| α-helix | 358-367 | 10 | |
| β-strand | 373-375 | 3 | 9 |
| α-helix | 389-401 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Putative heat shock protein | A, B | protein | 409 | Chaetomium thermophilum var. thermophilum DSM 1495 | G0RZX9 (AlphaFold model) |
>4GNI_1 Putative heat shock protein (chains A, B) MAESASKAAPGERVVIGITFGNSNSSIAHTVDDKAEVIANEDGDRQIPTILSYVDGDEYY GQQAKNFLVRNPKNTVAYFRDILGQDFKSVDPTHNHASAHPQEAGDNVVFTIKDKAEEDA EPSTLTVSEIATRYLRRLVGAASEYLGKKVTSAVITIPTNFTEKQKAALIAAAAAADLEV LQLISEPAAAVLAYDARPEATISDKIIVVADLGGSRSDVTVLASRSGMYTILATVHDYEY HGIALDKVLIDHFSKEFLKKNPGAKDPRENPRSLAKLRLEAESTKRALSRSTNASFSVES LIDGLDFASTINRLRYETIARTVFEGFNRLVESAVKKAGLDPLDVDEVIMSGGTSNTPRI AANFRYIFPESTRILAPSTDPSALNPSELQARGAALQASLIQEHHHHHH
Structural characterization of a eukaryotic chaperone-the ribosome-associated complex. Leidig, C., Bange, G., Kopp, J. et al. Nat Struct Mol Biol (2013) 20:23-28. DOI 10.1038/nsmb.2447 · PubMed
Other PDB entries of the same protein (UniProt G0RZX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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