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

Analyse Structure of cytochrome C551 from P. aeruginosa refined at 1.6 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 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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