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NMR structure of the Y48PCMF variant of human cytochrome C in its reduced state

Analyse NMR structure of the Y48PCMF variant of human cytochrome C in its reduced state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N3Y
Type: protein
Length: 104 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C
UniProt: P99999
Ligands: MH0
Pockets: 1 · best druggability 0.73

Structure

solution nmr · 1 distinct chain · 38% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C	protein	104	38% helix, 0% strand	P99999

Ligands and binding sites

MH0 · Mesoheme · ligand · 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	307	0.73	0.85	42	MH0

Modifications

Observed in the structure: 2 covalent, 1 modified (covalent ligand, nonstandard).

Compared structures

2N3Y · NMR structure of the Y48pCMF variant of human cytochrome c in its reduced state · 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 0.89

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 2N3Y · PDBe 2N3Y · UniProt P99999

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