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Oxidized structure of cytochrome C3 from desulfovibrio desulfuricans atcc 27774 at pH 7.6

Analyse Oxidized structure of cytochrome C3 from desulfovibrio desulfuricans atcc 27774… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UPD
Type: protein
Length: 107 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C3
UniProt: Q9L915
Ligands: HEC
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C3	protein	107	30% helix, 11% strand	Q9L915

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	760	0.77	0.81	72	HEC

Modifications

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

Compared structures

1UPD · Oxidized STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9L915
Elsewhere: RCSB PDB 1UPD · PDBe 1UPD · UniProt Q9L915

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