MolNFT v1 · #115948 · protein

Refinement of myoglobin and cytochrome C

5CYT: “Refinement of myoglobin and cytochrome C”. X-ray diffraction, 2 ligands (ACE, HEC), 1 pocket (best druggability 0.74). MolNFT v1 #115948 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CYT
Type: protein
Length: 103 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: P81459
Ligands: ACE, HEC
Pockets: 1 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
R	Cytochrome C	protein	103	41% helix, 2% strand	P81459

Ligands and binding sites

ACE · Acetyl group · ligand · chains R
HEC · Heme C · ligand · chains R

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	198	0.74	0.89	33	HEC

Modifications

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

Compared structures

5CYT · Refinement of myoglobin and cytochrome C · the same entry in another collection · chain R against R, TM-score 1.00
P81459 · AlphaFold monomer V2.0 prediction for cytochrome C (P81459) · a predicted model of the same protein · chain R 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 P81459
Elsewhere: RCSB PDB 5CYT · PDBe 5CYT · UniProt P81459

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