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Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment

Analyse Mutation of tyrosine-67 in cytochrome C significantly alters the local heme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CTY
Type: protein
Length: 108 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: P00044
Ligands: HEC, SO4
Pockets: 1 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C	protein	108	40% helix, 2% strand	P00044

Ligands and binding sites

HEC · Heme C · ligand · chains A
SO4 · Sulfate ion · ion · 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	255	0.81	0.92	40	HEC

Modifications

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

Compared structures

1CTY · Mutation of tyrosine-67 in cytochrome C significantly alters the local heme environment · the same entry in another collection · chain A against A, TM-score 1.00
P00044 · AlphaFold monomer V2.0 prediction for cytochrome C isoform 1 (P00044) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P00044
Elsewhere: RCSB PDB 1CTY · PDBe 1CTY · UniProt P00044

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