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Structure of ferrous horseradish peroxidase C1A

Analyse Structure of ferrous horseradish peroxidase C1A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1H58
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxidase C1A
EC: 1.11.1.7
UniProt: P00433
Ligands: HEM, CA
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxidase C1A (EC 1.11.1.7)	protein	306	49% helix, 5% strand	P00433

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	339	0.81	0.91	48	HEM
2	51	0.45	0.85	19	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1H58 · Structure of ferrous horseradish peroxidase C1A · the same entry in another collection · chain A against A, TM-score 1.00
P00433 · AlphaFold monomer V2.0 prediction for peroxidase C1A (P00433) · 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 P00433
Elsewhere: RCSB PDB 1H58 · PDBe 1H58 · UniProt P00433

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