Research workbench
Structure of geobacter sulfurreducens proline utilization a (puta) variant A206W
Analyse Structure of geobacter sulfurreducens proline utilization a (puta) variant A206W in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NA0
- Type
- protein
- Length
- 1,959 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein puta
- EC
- 1.5.5.2, 1.2.1.88
- UniProt
- Q746X3
- Ligands
- FAD, SO4
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein puta (EC 1.5.5.2, 1.2.1.88) | protein | 981 | 48% helix, 17% strand | Q746X3 |
| B | Bifunctional protein puta (EC 1.5.5.2, 1.2.1.88) | protein | 978 | 48% helix, 17% strand | Q746X3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 50 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1097 | 0.89 | 0.90 | 139 | FAD, SO4, EDO |
| 2 | 809 | 0.87 | 0.90 | 88 | FAD, SO4, EDO |
| 3 | 514 | 0.85 | 0.91 | 86 | EDO |
| 4 | 337 | 0.85 | 0.94 | 49 | EDO |
| 5 | 589 | 0.64 | 0.75 | 60 | EDO |
Interfaces
1 interface between chains.
- A–B · 4583 Ų buried · 78 hydrogen bonds · protein-protein
Compared structures
- 7NA0 · Structure of Geobacter sulfurreducens proline utilization A (PutA) variant A206W · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q746X3
- Elsewhere: RCSB PDB 7NA0 · PDBe 7NA0 · UniProt Q746X3
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