MolNFT v1 · #59936 · protein

Altering substrate specificity at the heme edge of cytochrome C peroxidase

3CCX: “Altering substrate specificity at the heme edge of cytochrome C peroxidase”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.84). MolNFT v1 #59936 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3CCX
Type: protein
Length: 291 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C peroxidase
EC: 1.11.1.5
UniProt: P00431
Ligands: HEM
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C peroxidase (EC 1.11.1.5)	protein	291	51% helix, 8% strand	P00431

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	330	0.84	0.94	43	HEM
2	85	0.42	0.79	17	empty

Compared structures

3CCX · Altering substrate specificity at the heme edge of cytochrome C peroxidase · the same entry in another collection · chain A against A, TM-score 1.00
P00431 · AlphaFold monomer V2.0 prediction for cytochrome C peroxidase, mitochondrial (P00431) · a predicted model of the same protein · 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 P00431
Elsewhere: RCSB PDB 3CCX · PDBe 3CCX · UniProt P00431

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