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Dihydrodipicolinate reductase from the industrial and evolutionarily important cyanobacteria Anabaena variabilis.

Analyse Dihydrodipicolinate reductase from the industrial and evolutionarily important… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KT0
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.83
Source: Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Molecule: 4-hydroxy-tetrahydrodipicolinate reductase
EC: 1.17.1.8
UniProt: Q3MFY8
Ligands: MG
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · resolution 2.83 · 1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8)	protein	274	34% helix, 24% strand	Q3MFY8

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

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	270	0.57	0.77	36	MG

Compared structures

5KT0 · Dihydrodipicolinate reductase from the industrial and evolutionarily important… · the same entry in another collection · chain A against A, TM-score 1.00
Q3MFY8 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (Q3MFY8) · a predicted model of the same protein · chain A against A, TM-score 0.90

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 Q3MFY8
Elsewhere: RCSB PDB 5KT0 · PDBe 5KT0 · UniProt Q3MFY8

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