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Structure of desulfovibrio desulfuricans G20 tetraheme cytochrome (oxidized form)

Analyse Structure of desulfovibrio desulfuricans G20 tetraheme cytochrome (oxidized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A3M
Type: protein
Length: 107 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: COG3005: NITRATE/TMAO reductases, membrane-bound tetraheme cytochrome C subunit
UniProt: Q30WH0
Ligands: HEC
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	COG3005: NITRATE/TMAO reductases, membrane-bound tetraheme cytochrome C subunit	protein	107	27% helix, 9% strand	Q30WH0

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	696	0.76	0.81	72	HEC

Modifications

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

Compared structures

2A3M · Structure of Desulfovibrio desulfuricans G20 tetraheme cytochrome (oxidized form) · 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 Q30WH0
Elsewhere: RCSB PDB 2A3M · PDBe 2A3M · UniProt Q30WH0

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