MolNFT v1 · #54351 · protein
Cytochrome C prime from alcaligenes xylosoxidans: ferrous R124E variant
2XM4 · Cytochrome C': “Cytochrome C prime from alcaligenes xylosoxidans: ferrous R124E variant”. X-ray diffraction, 1 ligand (HEC), 1 pocket (best druggability 0.63). MolNFT v1 #54351 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2XM4
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C'
- UniProt
- P00138
- Ligands
- HEC
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C' | protein | 127 | 73% helix, 2% strand | P00138 |
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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.63 | 0.83 | 28 | HEC |
Modifications
Observed in the structure: 2 cofactor, 1 modified (heme c attachment, cyclization).
Compared structures
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 P00138
- Elsewhere: RCSB PDB 2XM4 · PDBe 2XM4 · UniProt P00138
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