The bicyclic intermediate structure provides insights into the desuccinylation mechanism of SIRT5. Determined by X-ray diffraction at 1.7 Å resolution. Released 20 Jun 2012.
Explore 4F56 in 3D Show helices and sheets RCSB PDB PDBe
4F56 contains 37 α-helices and 36 β-strands across 4 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 | 37 | 1 | 1 |
| α-helix | 40-49 | 10 | |
| β-strand | 52-57 | 6 | 1 |
| α-helix | 59-61 | 3 | |
| α-helix | 63-65 | 3 | |
| β-strand | 77 | 1 | 2 |
| β-strand | 80 | 1 | 2 |
| α-helix | 82-85 | 4 | |
| α-helix | 88-93 | 6 | |
| α-helix | 95-110 | 16 | |
| α-helix | 116-130 | 15 | |
| β-strand | 134-139 | 6 | 1 |
| α-helix | 145-149 | 5 | |
| β-strand | 154-156 | 3 | 1 |
| β-strand | 159-166 | 8 | 3 |
| β-strand | 172-174 | 3 | 3 |
| α-helix | 182-184 | 3 | |
| α-helix | 194-196 | 3 | |
| α-helix | 201-203 | 3 | |
| β-strand | 206 | 1 | 4 |
| α-helix | 214 | 1 | |
| β-strand | 215 | 1 | 4 |
| β-strand | 216-220 | 5 | 3 |
| α-helix | 221-222 | 2 | |
| β-strand | 226 | 1 | 5 |
| α-helix | 227-228 | 2 | |
| α-helix | 229-241 | 13 | |
| β-strand | 244-248 | 5 | 1 |
| β-strand | 255 | 1 | 6 |
| α-helix | 257-259 | 3 | |
| α-helix | 260-266 | 7 | |
| β-strand | 271-275 | 5 | 1 |
| α-helix | 282-284 | 3 | |
| β-strand | 287-290 | 4 | 1 |
| α-helix | 293-301 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37 | 1 | 7 |
| α-helix | 40-49 | 10 | |
| β-strand | 52-57 | 6 | 7 |
| α-helix | 59-61 | 3 | |
| α-helix | 63-65 | 3 | |
| β-strand | 77 | 1 | 8 |
| β-strand | 80 | 1 | 8 |
| α-helix | 82-85 | 4 | |
| α-helix | 88-93 | 6 | |
| α-helix | 95-109 | 15 | |
| α-helix | 116-129 | 14 | |
| β-strand | 134-139 | 6 | 7 |
| α-helix | 145-149 | 5 | |
| β-strand | 154-156 | 3 | 7 |
| β-strand | 159-166 | 8 | 9 |
| β-strand | 172-174 | 3 | 9 |
| α-helix | 182-184 | 3 | |
| α-helix | 201-203 | 3 | |
| β-strand | 206 | 1 | 10 |
| α-helix | 214 | 1 | |
| β-strand | 215 | 1 | 10 |
| β-strand | 216-220 | 5 | 9 |
| α-helix | 221-222 | 2 | |
| β-strand | 226 | 1 | 11 |
| α-helix | 227-228 | 2 | |
| α-helix | 229-241 | 13 | |
| β-strand | 244-248 | 5 | 7 |
| β-strand | 255 | 1 | 12 |
| α-helix | 257-259 | 3 | |
| α-helix | 260-266 | 7 | |
| β-strand | 271-275 | 5 | 7 |
| α-helix | 282-284 | 3 | |
| β-strand | 287-290 | 4 | 7 |
| α-helix | 293-300 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8 | 1 | 5 |
| β-strand | 10 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial | A, B | protein | 273 | Homo sapiens | Q9NXA8 (AlphaFold model) |
| peptide from Histone H3.1 | C, D | protein | 12 | Homo sapiens | P68431 (AlphaFold model) |
>4F56_1 NAD-dependent lysine demalonylase and desuccinylase sirtuin-5, mitochondrial (chains A, B) GSFTARPSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPL AFAHNPSRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKA GTKNLLEIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEE AGCGGLLRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGV PVAEFNTETTPATNRFRFHFQGPCGTTLPEALA
>4F56_2 peptide from Histone H3.1 (chains C, D) KQTARKSTGGKA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
| CGK | 3-[(2R,3aR,5R,6R,6aR)-5-({[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-… | C19 H27 N5 O16 P2 S | 2 |
The Bicyclic Intermediate Structure Provides Insights into the Desuccinylation Mechanism of Human Sirtuin 5 (SIRT5). Zhou, Y., Zhang, H., He, B. et al. J Biol Chem (2012) 287:28307-28314. DOI 10.1074/jbc.M112.384511 · PubMed
Other PDB entries of the same protein (UniProt Q9NXA8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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