Research workbench

Chloroperoxidase F/PROPIONATE complex

Analyse Chloroperoxidase F/PROPIONATE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A8S
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloroperoxidase F
EC: 1.11.1.10
UniProt: O31158
Ligands: SO4
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloroperoxidase F (EC 1.11.1.10)	protein	273	45% helix, 17% strand	O31158

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A
PPI · Propanoic acid · additive · 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	93	0.58	0.86	20	PPI

Compared structures

1A8S · Chloroperoxidase F/PROPIONATE complex · the same entry in another collection · chain A against A, TM-score 1.00
O31158 · AlphaFold monomer V2.0 prediction for non-heme chloroperoxidase (O31158) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O31158
Elsewhere: RCSB PDB 1A8S · PDBe 1A8S · UniProt O31158

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