MolNFT v1 · #31348 · protein
Cytochrome C peroxidase in complex with phenol
2AS3 · Cytochrome C peroxidase, mitochondrial: “Cytochrome C peroxidase in complex with phenol”. X-ray diffraction, 3 ligands (HEM, IPH, K), 2 pockets (best druggability 0.81). MolNFT v1 #31348 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2AS3
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome C peroxidase, mitochondrial
- EC
- 1.11.1.5
- UniProt
- P00431
- Ligands
- HEM, IPH, K
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome C peroxidase, mitochondrial (EC 1.11.1.5) | protein | 291 | 51% helix, 8% strand | P00431 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- IPH · Phenol · ligand · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.81 | 0.89 | 52 | K, HEM, IPH |
| 2 | 94 | 0.41 | 0.78 | 17 | empty |
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 P00431
- Elsewhere: RCSB PDB 2AS3 · PDBe 2AS3 · UniProt P00431
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