MolNFT v1 · #4562 · protein

Escherichia COLI DHPR/NADH complex

1DRU · Dihydrodipicolinate reductase: “Escherichia COLI DHPR/NADH complex”. X-ray diffraction, 1 ligand (NAD), 2 pockets (best druggability 0.66). MolNFT v1 #4562 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1DRU
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate reductase
EC: 1.3.1.26
UniProt: P04036
Ligands: NAD
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrodipicolinate reductase (EC 1.3.1.26)	protein	270	34% helix, 22% strand	P04036

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · 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	456	0.66	0.78	46	NAD
2	67	0.31	0.75	16	empty

Compared structures

1DRU · Escherichia COLI DHPR/NADH complex · the same entry in another collection · chain A against A, TM-score 1.00
P04036 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (P04036) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P04036
Elsewhere: RCSB PDB 1DRU · PDBe 1DRU · UniProt P04036

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