Research workbench
Crystal structure of putidaredoxin reductase from pseudomonas putida
Analyse Crystal structure of putidaredoxin reductase from pseudomonas putida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q1W
- Type
- protein
- Length
- 843 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putidaredoxin reductase
- EC
- 1.18.1.-
- UniProt
- P16640
- Ligands
- FAD
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putidaredoxin reductase (EC 1.18.1.-) | protein | 422 | 28% helix, 28% strand | P16640 |
| B | Putidaredoxin reductase (EC 1.18.1.-) | protein | 421 | 28% helix, 29% strand | P16640 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1043 | 0.83 | 0.84 | 94 | FAD |
| 2 | 1182 | 0.82 | 0.83 | 109 | FAD |
| 3 | 320 | 0.60 | 0.78 | 36 | empty |
| 4 | 224 | 0.59 | 0.80 | 41 | empty |
| 5 | 163 | 0.59 | 0.82 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 1053 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1Q1W · Crystal Structure of Putidaredoxin Reductase from Pseudomonas putida · the same entry in another collection · chain A against A, TM-score 1.00
- P16640 · AlphaFold monomer V2.0 prediction for putidaredoxin reductase cama (P16640) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P16640
- Elsewhere: RCSB PDB 1Q1W · PDBe 1Q1W · UniProt P16640
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