MolNFT v1 · #5811 · protein

Crystal structure of cytochrome C4 from pseudomonas stutzeri

1ETP: “Crystal structure of cytochrome C4 from pseudomonas stutzeri”. X-ray diffraction, 1 ligand (HEM), 2 pockets (best druggability 0.86). MolNFT v1 #5811 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1ETP
Type: protein
Length: 380 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C4
UniProt: Q52369
Ligands: HEM
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome C4	protein	190	47% helix, 2% strand	Q52369

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B

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	1199	0.86	0.86	156	HEM
2	77	0.35	0.76	20	empty

Interfaces

1 interface between chains.

A–B · 505 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 cofactor (heme attachment).

Compared structures

1ETP · Crystal structure of cytochrome C4 from pseudomonas stutzeri · the same entry in another collection · chain A against A, TM-score 1.00
Q52369 · AlphaFold monomer V2.0 prediction for cytochrome C4 (Q52369) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q52369
Elsewhere: RCSB PDB 1ETP · PDBe 1ETP · UniProt Q52369

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