MolNFT v1 · #49926 · protein

Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)

2R37: “Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)”. X-ray diffraction, 2 ligands (NA, CL), 1 pocket (best druggability 0.61). MolNFT v1 #49926 on GenesisL1: 3D structure, binding sites and…

PDB: 2R37
Type: protein
Length: 379 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glutathione peroxidase 3
EC: 1.11.1.9
UniProt: P22352
Ligands: NA, CL
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutathione peroxidase 3 (EC 1.11.1.9)	protein	191	36% helix, 18% strand	P22352
B	Glutathione peroxidase 3 (EC 1.11.1.9)	protein	188	33% helix, 19% strand	P22352

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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	444	0.61	0.76	37	empty

Interfaces

1 interface between chains.

A–B · 238 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2R37 · Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant) · the same entry in another collection · 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 P22352
Elsewhere: RCSB PDB 2R37 · PDBe 2R37 · UniProt P22352

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