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Crystal structure of apo-dtdp-6-deoxy-L-lyxo-4-hexulose reductase (rmld) from salmonella enterica serovar typhimurium

Analyse Crystal structure of apo-dtdp-6-deoxy-L-lyxo-4-hexulose reductase (rmld) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KBZ
Type: protein
Length: 298 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dtdp-glucose oxidoreductase
EC: 1.1.1.133
UniProt: P26392
Ligands: MG
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dtdp-glucose oxidoreductase (EC 1.1.1.133)	protein	298	44% helix, 18% strand	P26392

Ligands and binding sites

MG · Magnesium 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	606	0.69	0.77	56	empty
2	86	0.43	0.79	23	empty

Compared structures

1KBZ · Crystal Structure of apo-dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) from Salmonella… · the same entry in another collection · chain A against A, TM-score 1.00
P26392 · AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose reductase (P26392) · 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 P26392
Elsewhere: RCSB PDB 1KBZ · PDBe 1KBZ · UniProt P26392

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