MolNFT v1 · #88459 · protein

Neutron structure of ferric cytochrome C peroxidase - deuterium exchanged at room temperature

4CVI · Cytochrome C peroxidase, mitochondrial: “Neutron structure of ferric cytochrome C peroxidase - deuterium exchanged at room temperature”. X-ray diffraction; neutron diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.81).…

PDB: 4CVI
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction; neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C peroxidase, mitochondrial
EC: 1.11.1.5
UniProt: D6VXC7
Ligands: HEM
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction; neutron diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C peroxidase, mitochondrial (EC 1.11.1.5)	protein	292	50% helix, 8% strand	D6VXC7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.81	0.89	45	HEM
2	93	0.41	0.78	16	empty

Compared structures

4CVI · Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room… · 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 D6VXC7
Elsewhere: RCSB PDB 4CVI · PDBe 4CVI · UniProt D6VXC7

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