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Crystal structure of a novel aldo keto reductase TM1743 from thermotoga maritima in complex with NADP+

Analyse Crystal structure of a novel aldo keto reductase TM1743 from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DAN
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,5-diketo-D-gluconic acid reductase
EC: 1.1.1.-
UniProt: Q9X265
Ligands: NAP
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2,5-diketo-D-gluconic acid reductase (EC 1.1.1.-)	protein	274	47% helix, 19% strand	Q9X265

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	248	0.60	0.79	32	NAP
2	57	0.30	0.75	13	empty

Compared structures

5DAN · Crystal structure of a novel aldo keto reductase Tm1743 from Thermotoga maritima in… · 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 Q9X265
Elsewhere: RCSB PDB 5DAN · PDBe 5DAN · UniProt Q9X265

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