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Structure of glyoxylate reductase 1 from arabidopsis (ATGLYR1)

Analyse Structure of glyoxylate reductase 1 from arabidopsis (ATGLYR1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DOJ
Type: protein
Length: 292 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehydrogenase-like protein
EC: 1.1.1.79
UniProt: Q9LSV0
Ligands: CL
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dehydrogenase-like protein (EC 1.1.1.79)	protein	292	57% helix, 14% strand	Q9LSV0

Ligands and binding sites

CL · Chloride ion · ion · chains A

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	393	0.67	0.80	47	empty

Compared structures

3DOJ · Structure of Glyoxylate reductase 1 from Arabidopsis (AtGLYR1) · the same entry in another collection · chain A against A, TM-score 1.00
Q9LSV0 · AlphaFold monomer V2.0 prediction for GLYOXYLATE/SUCCINIC semialdehyde reductase 1… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9LSV0
Elsewhere: RCSB PDB 3DOJ · PDBe 3DOJ · UniProt Q9LSV0

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