Research workbench
Crystal structure of a putative chromate reductase from gluconacetobacter hansenii, gh-chrr, containing a R101A substitution.
Analyse Crystal structure of a putative chromate reductase from gluconacetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H6P
- Type
- protein
- Length
- 2,208 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromate reductase
- UniProt
- D5QFC5
- Ligands
- FMN
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Chromate reductase | protein | 184 | 42% helix, 20% strand | D5QFC5 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 12 copies · chains A, B, C, D, E, F, G, L, H, I, J, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.86 | 0.96 | 61 | empty |
| 2 | 212 | 0.83 | 0.96 | 43 | empty |
| 3 | 105 | 0.76 | 0.96 | 22 | empty |
| 4 | 945 | 0.76 | 0.79 | 66 | FMN |
| 5 | 132 | 0.74 | 0.93 | 23 | empty |
Interfaces
19 interfaces between chains.
- G–L · 1444 Ų buried · 23 hydrogen bonds · protein-protein
- H–I · 1431 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1422 Ų buried · 24 hydrogen bonds · protein-protein
- J–K · 1413 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1410 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 4H6P · Crystal structure of a putative chromate reductase from Gluconacetobacter hansenii… · 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 D5QFC5
- Elsewhere: RCSB PDB 4H6P · PDBe 4H6P · UniProt D5QFC5
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