MolNFT v1 · #141844 · protein

Solution structure of molten globule state of L94G mutant of horse cytochrome-C

5ZKV · Cytochrome C: “Solution structure of molten globule state of L94G mutant of horse cytochrome-C”. Solution nmr, 1 ligand (HEC), 2 pockets (best druggability 0.78). MolNFT v1 #141844 on GenesisL1: 3D structure, binding sites and…

PDB: 5ZKV
Type: protein
Length: 104 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: P00004
Ligands: HEC
Pockets: 2 · best druggability 0.78

Structure

solution nmr · 1 distinct chain · 45% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C	protein	104	45% helix, 0% strand	P00004

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	517	0.78	0.85	43	HEC
2	104	0.38	0.75	25	empty

Modifications

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

Compared structures

5ZKV · Solution structure of molten globule state of L94G mutant of horse cytochrome-c · the same entry in another collection · chain A against A, TM-score 1.00
P00004 · AlphaFold monomer V2.0 prediction for cytochrome C (P00004) · a predicted model of the same protein · chain A against A, TM-score 0.66

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 P00004
Elsewhere: RCSB PDB 5ZKV · PDBe 5ZKV · UniProt P00004

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