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Crystal structure of cytochrome C3 from desulfovibrio desulfuricans norway at 1.7 ångströms resolution

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

PDB: 2CY3
Type: protein
Length: 118 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C3
UniProt: P00136
Ligands: HEC
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C3	protein	118	25% helix, 7% strand	P00136

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

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	613	0.75	0.82	68	HEC
2	76	0.50	0.84	20	HEC

Modifications

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

Compared structures

2CY3 · Crystal structure of cytochrome C3 from desulfovibrio desulfuricans norway at 1.7… · the same entry in another collection · chain A against A, TM-score 1.00
P00136 · AlphaFold monomer V2.0 prediction for cytochrome C3, 13 kda (P00136) · a predicted model of the same protein · chain A against A, TM-score 0.99

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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 P00136
Elsewhere: RCSB PDB 2CY3 · PDBe 2CY3 · UniProt P00136

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