Research workbench
Crystal structure of putative NAD(P)H-flavin oxidoreductase from haemophilus influenzae 86-028NP
Analyse Crystal structure of putative NAD(P)H-flavin oxidoreductase from haemophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S14
- Type
- protein
- Length
- 883 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative NAD(P)H nitroreductase
- EC
- 1.-.-.-
- UniProt
- Q4QJZ7
- Ligands
- FMN, K, CA, CL
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative NAD(P)H nitroreductase (EC 1.-.-.-) | protein | 219 | 49% helix, 16% strand | Q4QJZ7 |
| B | Putative NAD(P)H nitroreductase (EC 1.-.-.-) | protein | 223 | 50% helix, 16% strand | Q4QJZ7 |
| C | Putative NAD(P)H nitroreductase (EC 1.-.-.-) | protein | 220 | 50% helix, 16% strand | Q4QJZ7 |
| D | Putative NAD(P)H nitroreductase (EC 1.-.-.-) | protein | 221 | 50% helix, 16% strand | Q4QJZ7 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
- K · Potassium ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B, C, D
- CL · Chloride ion · ion · 3 copies · chains A, B, C
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.71 | 0.84 | 45 | FMN, CL, EDO |
| 2 | 436 | 0.71 | 0.82 | 45 | FMN, CL, EDO |
| 3 | 470 | 0.69 | 0.80 | 44 | FMN |
| 4 | 594 | 0.68 | 0.78 | 79 | empty |
| 5 | 383 | 0.68 | 0.81 | 42 | EDO, FMN, CL |
Interfaces
3 interfaces between chains.
- C–D · 4421 Ų buried · 76 hydrogen bonds · protein-protein
- A–B · 4377 Ų buried · 71 hydrogen bonds · protein-protein
- B–C · 246 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 27 modified (engineered).
Compared structures
- 7S14 · Crystal structure of putative NAD(P)H-flavin oxidoreductase from Haemophilus influenzae… · 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 Q4QJZ7
- Elsewhere: RCSB PDB 7S14 · PDBe 7S14 · UniProt Q4QJZ7
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