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Cytochrome C peroxidase W191G in complex with 1-methyl-2-vinyl- pyridinium

Analyse Cytochrome C peroxidase W191G in complex with 1-methyl-2-vinyl- pyridinium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RC2
Type: protein
Length: 292 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: A7A026
Ligands: HEM, 286
Pockets: 2 · best druggability 0.82

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Cytochrome C peroxidase (EC 1.11.1.5)	protein	292	50% helix, 8% strand	A7A026

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains X
286 · 2-ethenyl-1-methylpyridinium · ligand · chains X

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	406	0.82	0.90	56	HEM, 286
2	93	0.40	0.77	20	empty

Compared structures

2RC2 · Cytochrome C Peroxidase W191G in complex with 1-methyl-2-vinyl-pyridinium · the same entry in another collection · chain X against X, 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 A7A026
Elsewhere: RCSB PDB 2RC2 · PDBe 2RC2 · UniProt A7A026

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