MolNFT v1 · #19568 · protein

Arabidopsis thaliana peroxidase A2 at room temperature

1QO4: “Arabidopsis thaliana peroxidase A2 at room temperature”. X-ray diffraction, 2 ligands (HEM, CA), 2 pockets (best druggability 0.80). MolNFT v1 #19568 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QO4
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peroxidase
EC: 1.11.1.7
UniProt: Q42578
Ligands: HEM, CA
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peroxidase (EC 1.11.1.7)	protein	306	50% helix, 4% strand	Q42578

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CA · Calcium ion · metal · 2 copies · 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	361	0.80	0.90	52	HEM
2	55	0.28	0.74	15	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1QO4 · Arabidopsis thaliana peroxidase A2 at room temperature · the same entry in another collection · chain A against A, TM-score 1.00
Q42578 · AlphaFold monomer V2.0 prediction for peroxidase 53 (Q42578) · 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 Q42578
Elsewhere: RCSB PDB 1QO4 · PDBe 1QO4 · UniProt Q42578

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