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Solution structure of FE(II) cytochrome C551 from pseudomonas aeruginosa as determined by two-dimensional 1H NMR

Analyse Solution structure of FE(II) cytochrome C551 from pseudomonas aeruginosa as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PAC
Type: protein
Length: 82 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome C551
UniProt: P00099
Ligands: HEC
Pockets: 1 · best druggability 0.68

Structure

solution nmr · 1 distinct chain · 32% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome C551	protein	82	32% helix, 0% strand	P00099

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	298	0.68	0.82	36	HEC

Modifications

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

Compared structures

2PAC · Solution structure of FE(II) cytochrome C551 from pseudomonas aeruginosa as determined by… · 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 0.79

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 2PAC · PDBe 2PAC · UniProt P00099

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