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The apo-structure of D-lactate dehydrogenase from pseudomonas aeruginosa

Analyse The apo-structure of D-lactate dehydrogenase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ABJ
Type: protein
Length: 657 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-lactate dehydrogenase (fermentative)
UniProt: Q9I530
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-lactate dehydrogenase (fermentative)	protein	328	40% helix, 17% strand	Q9I530
B	D-lactate dehydrogenase (fermentative)	protein	329	40% helix, 17% strand	Q9I530

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A, B

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	355	0.65	0.80	41	ACT
2	312	0.62	0.79	41	ACT

Interfaces

1 interface between chains.

A–B · 2795 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

6ABJ · The apo-structure of D-lactate dehydrogenase from Pseudomonas aeruginosa · 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 Q9I530
Elsewhere: RCSB PDB 6ABJ · PDBe 6ABJ · UniProt Q9I530

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