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Chloroperoxidase L

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

PDB: 1A88
Type: protein
Length: 825 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloroperoxidase L
EC: 1.11.1.10
UniProt: P49323
Pockets: 9 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Chloroperoxidase L (EC 1.11.1.10)	protein	275	43% helix, 18% strand	P49323

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	642	0.74	0.81	54	empty
2	57	0.68	0.96	21	empty
3	56	0.67	0.96	20	empty
4	144	0.56	0.81	21	empty
5	54	0.51	0.86	20	empty

Interfaces

3 interfaces between chains.

A–B · 763 Å² buried · 12 hydrogen bonds · protein-protein
A–C · 758 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 733 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1A88 · Chloroperoxidase L · the same entry in another collection · chain A against A, TM-score 1.00
P49323 · AlphaFold monomer V2.0 prediction for non-heme chloroperoxidase (P49323) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 P49323
Elsewhere: RCSB PDB 1A88 · PDBe 1A88 · UniProt P49323

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