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Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from thermotoga maritima at 2.00 a resolution

Analyse Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1O20
Type: protein
Length: 414 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gamma-glutamyl phosphate reductase
EC: 1.2.1.41
UniProt: Q9WYC9
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gamma-glutamyl phosphate reductase (EC 1.2.1.41)	protein	414	45% helix, 18% strand	Q9WYC9

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	562	0.64	0.76	54	empty

Modifications

Observed in the structure: 2 modified (engineered).

Compared structures

1O20 · Crystal structure of Gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima… · the same entry in another collection · chain A against A, TM-score 1.00
Q9WYC9 · AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase (Q9WYC9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9WYC9
Elsewhere: RCSB PDB 1O20 · PDBe 1O20 · UniProt Q9WYC9

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