Research workbench

Crystal structure of cytochrome C2 mutant G95E

Analyse Crystal structure of cytochrome C2 mutant G95E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VYD
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C2
UniProt: P00094
Ligands: HEM
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome C2	protein	116	40% helix, 6% strand	P00094

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	235	0.75	0.88	37	HEM
2	236	0.73	0.87	35	HEM
3	205	0.58	0.80	37	empty

Interfaces

1 interface between chains.

A–B · 323 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1VYD · Crystal structure of cytochrome C2 mutant G95E · the same entry in another collection · chain A against A, TM-score 1.00
P00094 · AlphaFold monomer V2.0 prediction for cytochrome C2 (P00094) · a predicted model of the same protein · chain B 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 P00094
Elsewhere: RCSB PDB 1VYD · PDBe 1VYD · UniProt P00094

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.