Research workbench

Solution structure of desulfovibrio gigas ferricytochrome C3, NMR, 15 structures

Analyse Solution structure of desulfovibrio gigas ferricytochrome C3, NMR, 15 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QN1
Type: protein
Length: 112 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C3
UniProt: P00133
Ligands: HEC
Pockets: 1 · best druggability 0.73

Structure

solution nmr · 1 distinct chain · 15% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C3	protein	112	15% helix, 10% strand	P00133

Ligands and binding sites

HEC · Heme C · ligand · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	730	0.73	0.79	75	HEC

Modifications

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

Compared structures

1QN1 · Solution structure of desulfovibrio gigas ferricytochrome C3, NMR, 15 structures · the same entry in another collection · chain A against A, TM-score 1.00
P00133 · AlphaFold monomer V2.0 prediction for cytochrome C3 (P00133) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P00133
Elsewhere: RCSB PDB 1QN1 · PDBe 1QN1 · UniProt P00133

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.