Research workbench
A131Q mutant of cyt P460 of nitrosomonas sp. AL212
Analyse A131Q mutant of cyt P460 of nitrosomonas sp. AL212 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E0Z
- Type
- protein
- Length
- 639 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P460
- UniProt
- F9ZFJ0
- Ligands
- HEC
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P460 | protein | 159 | 22% helix, 36% strand | F9ZFJ0 |
| B, D | Cytochrome P460 | protein | 161 | 22% helix, 36% strand | F9ZFJ0 |
| C | Cytochrome P460 | protein | 158 | 22% helix, 36% strand | F9ZFJ0 |
Ligands and binding sites
- HEC · Heme C · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.72 | 0.90 | 30 | HEC |
| 2 | 154 | 0.71 | 0.89 | 31 | HEC |
| 3 | 197 | 0.71 | 0.87 | 31 | HEC |
| 4 | 208 | 0.70 | 0.87 | 35 | HEC |
| 5 | 215 | 0.53 | 0.77 | 27 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1697 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1673 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 253 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 72 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 cofactor (heme c attachment).
Compared structures
- 6E0Z · A131Q mutant of cyt P460 of Nitrosomonas sp. AL212 · the same entry in another collection · chain C against C, 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 F9ZFJ0
- Elsewhere: RCSB PDB 6E0Z · PDBe 6E0Z · UniProt F9ZFJ0
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