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CRYSTAL STRUCTURE OF E.coli ALCOHOL DEHYDROGENASE - FucO MUTANT L259V

Analyse CRYSTAL STRUCTURE OF E.coli ALCOHOL DEHYDROGENASE - FucO MUTANT L259V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QNI
Type: protein
Length: 387 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.73
Source: Escherichia coli str. K-12 substr. MG1655
Molecule: Lactaldehyde reductase
EC: 1.1.1.77
UniProt: P0A9S2
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · resolution 1.73 · 1 distinct chain · 58% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
AAA	Lactaldehyde reductase (EC 1.1.1.77)	protein	387	58% helix, 12% strand	P0A9S2

Ligands and binding sites

CIT · Citric acid · additive · chains AAA

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	537	0.61	0.74	47	empty
2	81	0.60	0.88	21	empty

Compared structures

P0A9S2 · AlphaFold monomer V2.0 prediction for lactaldehyde reductase (P0A9S2) · a predicted model of the same protein · chain AAA against A, TM-score 0.86

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 P0A9S2
Elsewhere: RCSB PDB 7QNI · PDBe 7QNI · UniProt P0A9S2

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