MolNFT v1 · #51192 · protein

Structure of the arabidopsis thaliana cytochrome C6A V52Q variant

2V07: “Structure of the arabidopsis thaliana cytochrome C6A V52Q variant”. X-ray diffraction, 1 ligand (HEC), 1 pocket (best druggability 0.65). MolNFT v1 #51192 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2V07
Type: protein
Length: 98 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C6
UniProt: Q93VA3
Ligands: HEC
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C6	protein	98	51% helix, 6% strand	Q93VA3

Ligands and binding sites

HEC · Heme C · ligand · 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	203	0.65	0.84	29	HEC

Modifications

Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).

Compared structures

2V07 · Structure of the Arabidopsis thaliana cytochrome c6A V52Q variant · the same entry in another collection · chain A against A, TM-score 1.00
Q93VA3 · AlphaFold monomer V2.0 prediction for cytochrome C6, chloroplastic (Q93VA3) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q93VA3
Elsewhere: RCSB PDB 2V07 · PDBe 2V07 · UniProt Q93VA3

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