Human SIRT5 bound to Succ-IDH2 and Carba-NAD. Determined by X-ray diffraction at 1.94 Å resolution. Released 15 Aug 2012.
Explore 4G1C in 3D Show helices and sheets RCSB PDB PDBe
4G1C 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 | 60-63 | 4 | |
| α-helix | 72-75 | 4 | |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 80-81 | 2 | 2 |
| α-helix | 82-85 | 4 | |
| α-helix | 88-93 | 6 | |
| α-helix | 95-111 | 17 | |
| 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 | 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 | 293-300 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37 | 1 | 7 |
| α-helix | 40-49 | 10 | |
| β-strand | 52-57 | 6 | 7 |
| α-helix | 59-62 | 4 | |
| α-helix | 63-65 | 3 | |
| β-strand | 76-77 | 2 | 8 |
| β-strand | 80-81 | 2 | 8 |
| α-helix | 82-85 | 4 | |
| α-helix | 88-93 | 6 | |
| α-helix | 95-108 | 14 | |
| α-helix | 116-130 | 15 | |
| 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 | 194-196 | 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 | 293-301 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 4 | 1 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAD-dependent protein deacylase sirtuin-5, mitochondrial | A, B | protein | 267 | Homo sapiens | Q9NXA8 (AlphaFold model) |
| Succinylated IDH2 peptide | D, E | protein | 7 |
>4G1C_1 NAD-dependent protein deacylase sirtuin-5, mitochondrial (chains A, B) PSSSMADFRKFFAKAKHIVIISGAGVSAESGVPTFRGAGGYWRKWQAQDLATPLAFAHNP SRVWEFYHYRREVMGSKEPNAGHRAIAECETRLGKQGRRVVVITQNIDELHRKAGTKNLL EIHGSLFKTRCTSCGVVAENYKSPICPALSGKGAPEPGTQDASIPVEKLPRCEEAGCGGL LRPHVVWFGENLDPAILEEVDRELAHCDLCLVVGTSSVVYPAAMFAPQVAARGVPVAEFN TETTPATNRFRFHFQGPCGTTLPEALA
>4G1C_2 Succinylated IDH2 peptide (chains D, E) XAVXCAX
Synthesis of Carba-NAD and the Structures of Its Ternary Complexes with SIRT3 and SIRT5. Szczepankiewicz, B.G., Dai, H., Koppetsch, K.J. et al. J Org Chem (2012) 77:7319-7329. DOI 10.1021/jo301067e · 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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