MolNFT v1 · #9755 · protein

Solution structure of the functional domain of paracoccus denitrificans cytochrome C552 in the oxidized state

1I6E: “Solution structure of the functional domain of paracoccus denitrificans cytochrome C552 in the oxidized state”. Solution nmr, 1 ligand (HEC), 1 pocket (best druggability 0.75). MolNFT v1 #9755 on GenesisL1: 3D structure, binding…

PDB: 1I6E
Type: protein
Length: 100 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C552
UniProt: P54820
Ligands: HEC
Pockets: 1 · best druggability 0.75

Structure

solution nmr · 1 distinct chain · 40% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C552	protein	100	40% helix, 4% strand	P54820

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

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	199	0.75	0.90	32	HEC

Modifications

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

Compared structures

1I6E · Solution structure of the functional domain of paracoccus denitrificans cytochrome C552… · the same entry in another collection · chain A against A, TM-score 1.00
P54820 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P54820) · 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 P54820
Elsewhere: RCSB PDB 1I6E · PDBe 1I6E · UniProt P54820

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