MolNFT v1 · #116315 · protein

Crystal structure of dehydroascorbate reductase (osdhar) from oryza sativa L. japonica

5D9T: “Crystal structure of dehydroascorbate reductase (osdhar) from oryza sativa L. japonica”. X-ray diffraction, 1 ligand (NA), 2 pockets (best druggability 0.38). MolNFT v1 #116315 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5D9T
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dehydroascorbate reductase
UniProt: Q65XA0
Ligands: NA
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dehydroascorbate reductase	protein	211	53% helix, 12% strand	Q65XA0

Ligands and binding sites

NA · Sodium ion · metal · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	97	0.38	0.76	19	empty
2	53	0.30	0.75	13	empty

Compared structures

5D9T · Crystal structure of dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica · the same entry in another collection · chain A against A, TM-score 1.00
Q65XA0 · AlphaFold monomer V2.0 prediction for probable glutathione S-transferase DHAR1, cytosolic… · 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 Q65XA0
Elsewhere: RCSB PDB 5D9T · PDBe 5D9T · UniProt Q65XA0

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