MolNFT v1 · #107750 · protein

Cytochrome C prime from shewanella frigidimarina

4ULV · Cytochrome C, class II: “Cytochrome C prime from shewanella frigidimarina”. X-ray diffraction, 2 ligands (HEC, SO4), 2 pockets (best druggability 0.65). MolNFT v1 #107750 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4ULV
Type: protein
Length: 256 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C, class II
UniProt: Q07Z15
Ligands: HEC, SO4
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome C, class II	protein	128	71% helix, 2% strand	Q07Z15

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 3 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.65	0.85	26	HEC
2	163	0.62	0.84	21	HEC

Interfaces

1 interface between chains.

A–B · 741 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

4ULV · Cytochrome c prime from Shewanella frigidimarina · 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 Q07Z15
Elsewhere: RCSB PDB 4ULV · PDBe 4ULV · UniProt Q07Z15

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