MolNFT v1 · #118298 · protein

Human cytochrome C Y48H

5EXQ: “Human cytochrome C Y48H”. X-ray diffraction, 2 ligands (HEC, SO4), 2 pockets (best druggability 0.77). MolNFT v1 #118298 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5EXQ
Type: protein
Length: 208 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: P99999
Ligands: HEC, SO4
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cytochrome C	protein	104	41% helix, 2% strand	P99999

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains B

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	278	0.77	0.89	45	HEC
2	177	0.75	0.91	34	HEC

Interfaces

1 interface between chains.

A–B · 417 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

5EXQ · Human cytochrome c Y48H · the same entry in another collection · chain A against A, TM-score 1.00
P99999 · AlphaFold monomer V2.0 prediction for cytochrome C (P99999) · 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 P99999
Elsewhere: RCSB PDB 5EXQ · PDBe 5EXQ · UniProt P99999

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