MolNFT v1 · #151266 · protein

Cytochrome C prime beta from methylococcus capsulatus (bath)

6HIH: “Cytochrome C prime beta from methylococcus capsulatus (bath)”. X-ray diffraction, 3 ligands (HEC, ZN, SO4), 2 pockets (best druggability 0.65). MolNFT v1 #151266 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HIH
Type: protein
Length: 272 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: G1UBD5
Ligands: HEC, ZN, SO4
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome C	protein	136	22% helix, 36% strand	G1UBD5

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 2 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	289	0.65	0.81	32	HEC
2	272	0.65	0.81	29	HEC

Interfaces

1 interface between chains.

A–B · 1226 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

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

Compared structures

6HIH · Cytochrome c prime beta from Methylococcus capsulatus (Bath) · 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 G1UBD5
Elsewhere: RCSB PDB 6HIH · PDBe 6HIH · UniProt G1UBD5

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