MolNFT v1 · #159380 · protein
Crystal structure of C-type cytochrome xoxg from methylobacterium extorquens AM1
6ONQ · Cytochrome C xoxg: “Crystal structure of C-type cytochrome xoxg from methylobacterium extorquens AM1”. X-ray diffraction, 1 ligand (HEC), 3 pockets (best druggability 0.67). MolNFT v1 #159380 on GenesisL1: 3D structure, binding…
- PDB
- 6ONQ
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C xoxg
- UniProt
- P71510
- Ligands
- HEC
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C xoxg | protein | 159 | 43% helix, 11% strand | P71510 |
Ligands and binding sites
- HEC · Heme C · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.67 | 0.84 | 29 | HEC |
| 2 | 91 | 0.48 | 0.81 | 26 | empty |
| 3 | 77 | 0.36 | 0.77 | 21 | empty |
Modifications
Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).
Compared structures
- 6ONQ · Crystal structure of c-type cytochrome XoxG from Methylobacterium extorquens AM1 · 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 P71510
- Elsewhere: RCSB PDB 6ONQ · PDBe 6ONQ · UniProt P71510
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