Research workbench
Structure of cooa mutant (N127L/S128L) from carboxydothermus hydrogenoformans
Analyse Structure of cooa mutant (N127L/S128L) from carboxydothermus hydrogenoformans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HKX
- Type
- protein
- Length
- 366 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon monoxide oxidation system transcription regulator cooa-1
- UniProt
- Q3AB29
- Ligands
- HEM, CMO
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon monoxide oxidation system transcription regulator cooa-1 | protein | 218 | 39% helix, 28% strand | Q3AB29 |
| B | Carbon monoxide oxidation system transcription regulator cooa-1 | protein | 148 | 36% helix, 30% strand | Q3AB29 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A, B
- CMO · Carbon monoxide · ion · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.72 | 0.85 | 33 | HEM, CMO |
| 2 | 102 | 0.63 | 0.88 | 18 | empty |
| 3 | 145 | 0.59 | 0.83 | 26 | empty |
| 4 | 127 | 0.40 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1757 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2HKX · Structure of CooA mutant (N127L/S128L) from Carboxydothermus hydrogenoformans · 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 Q3AB29
- Elsewhere: RCSB PDB 2HKX · PDBe 2HKX · UniProt Q3AB29
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