MolNFT v1 · #85000 · protein

Structure of cytochrome C551 from P. aeruginosa refined at 1.6 ångströms resolution and comparison of the two redox forms

451C: “Structure of cytochrome C551 from P. aeruginosa refined at 1.6 ångströms resolution and comparison of the two…”. X-ray diffraction, 1 ligand (HEM), 1 pocket (best druggability 0.73). MolNFT v1 #85000 on GenesisL1: 3D structure…

PDB: 451C
Type: protein
Length: 82 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C551
UniProt: P00099
Ligands: HEM
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C551	protein	82	50% helix, 5% strand	P00099

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · 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	222	0.73	0.88	32	HEM

Modifications

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

Compared structures

451C · Structure of cytochrome C551 from P. aeruginosa refined at 1.6 ångströms resolution and… · the same entry in another collection · chain A against A, TM-score 1.00
P00099 · AlphaFold monomer V2.0 prediction for cytochrome C-551 (P00099) · 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 P00099
Elsewhere: RCSB PDB 451C · PDBe 451C · UniProt P00099

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