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The structure of haemophilus influenzae rd KW20 nitroreductase complexed with nicotinic acid
Analyse The structure of haemophilus influenzae rd KW20 nitroreductase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T33
- Type
- protein
- Length
- 438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative NAD(P)H nitroreductase
- EC
- 1.-.-.-
- UniProt
- Q57431
- Ligands
- FMN, NIO, SO4
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative NAD(P)H nitroreductase (EC 1.-.-.-) | protein | 219 | 47% helix, 16% strand | Q57431 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- NIO · Nicotinic acid · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 537 | 0.71 | 0.80 | 50 | FMN, NIO |
| 2 | 434 | 0.68 | 0.80 | 45 | NIO, FMN |
| 3 | 158 | 0.53 | 0.79 | 24 | empty |
| 4 | 168 | 0.52 | 0.79 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 4259 Ų buried · 62 hydrogen bonds · protein-protein
Compared structures
- 7T33 · The structure of Haemophilus influenzae Rd KW20 nitroreductase complexed with nicotinic… · the same entry in another collection · chain A against A, TM-score 1.00
- Q57431 · AlphaFold monomer V2.0 prediction for putative NAD(P)H nitroreductase (Q57431) · a predicted model of the same protein · chain A 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 Q57431
- Elsewhere: RCSB PDB 7T33 · PDBe 7T33 · UniProt Q57431
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