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Conformational mobility in the active site of a heme peroxidase

Analyse Conformational mobility in the active site of a heme peroxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GHH
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytosolic ascorbate peroxidase 1
EC: 1.11.1.11
UniProt: Q43758
Ligands: HEM, K, NO
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Cytosolic ascorbate peroxidase 1 (EC 1.11.1.11)	protein	250	53% helix, 2% strand	Q43758

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains X
K · Potassium ion · metal · chains X
NO · Nitric oxide · ion · chains X

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	403	0.78	0.87	54	HEM, NO

Compared structures

2GHH · Conformational mobility in the active site of a heme peroxidase · the same entry in another collection · chain X against X, 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 Q43758
Elsewhere: RCSB PDB 2GHH · PDBe 2GHH · UniProt Q43758

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