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Crystal structure of cytochrome C6 Q57V mutant from synechococcus sp. pcc 7002

Analyse Crystal structure of cytochrome C6 Q57V mutant from synechococcus sp. pcc 7002 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EID
Type: protein
Length: 93 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C6
UniProt: O30881
Ligands: HEC
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C6	protein	93	56% helix, 4% strand	O30881

Ligands and binding sites

HEC · Heme C · ligand · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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	252	0.72	0.86	36	HEC

Modifications

Observed in the structure: 2 cofactor (heme c attachment).

Compared structures

4EID · Crystal structure of cytochrome c6 Q57V mutant from Synechococcus sp. PCC 7002 · the same entry in another collection · chain A against A, TM-score 1.00
O30881 · AlphaFold monomer V2.0 prediction for cytochrome C6 (O30881) · 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 O30881
Elsewhere: RCSB PDB 4EID · PDBe 4EID · UniProt O30881

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