Research workbench
Structure of the shewanella loihica pv-4 NADH-dependent persulfide reductase F161A mutant
Analyse Structure of the shewanella loihica pv-4 NADH-dependent persulfide reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OCG
- Type
- protein
- Length
- 1,130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD-dependent pyridine nucleotide-disulphide oxidoreductase
- UniProt
- A3QAV3
- Ligands
- FAD, COA
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | FAD-dependent pyridine nucleotide-disulphide oxidoreductase | protein | 565 | 29% helix, 27% strand | A3QAV3 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- COA · Coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.86 | 0.87 | 130 | FAD, COA |
| 2 | 1153 | 0.86 | 0.87 | 141 | FAD, COA |
| 3 | 302 | 0.55 | 0.76 | 38 | empty |
| 4 | 65 | 0.53 | 0.87 | 18 | empty |
| 5 | 59 | 0.51 | 0.87 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3687 Ų buried · 56 hydrogen bonds · protein-protein
Compared structures
- 4OCG · Structure of the Shewanella loihica PV-4 NADH-dependent persulfide reductase F161A Mutant · 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 A3QAV3
- Elsewhere: RCSB PDB 4OCG · PDBe 4OCG · UniProt A3QAV3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.