MolNFT v1 · #13721 · protein

Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase

1LLD: “Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase”. X-ray diffraction, 1 ligand (NAD), 6 pockets (best druggability 0.70). MolNFT v1 #13721 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1LLD
Type: protein
Length: 626 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-lactate dehydrogenase
EC: 1.1.1.27
UniProt: P19869
Ligands: NAD
Pockets: 6 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L-lactate dehydrogenase (EC 1.1.1.27)	protein	313	45% helix, 19% strand	P19869

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	439	0.70	0.81	47	NAD
2	422	0.68	0.80	49	NAD
3	486	0.67	0.79	59	empty
4	165	0.52	0.79	22	empty
5	173	0.52	0.79	26	empty

Interfaces

1 interface between chains.

A–B · 1114 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1LLD · Molecular basis of allosteric activation of bacterial L-lactate dehydrogenase · 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 P19869
Elsewhere: RCSB PDB 1LLD · PDBe 1LLD · UniProt P19869

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