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Crystal structure of leishmania mexicana glycerol-3-phosphate dehydrogenase

Analyse Crystal structure of leishmania mexicana glycerol-3-phosphate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EVY
Type: protein
Length: 346 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycerol-3-phosphate dehydrogenase
EC: 1.1.1.8
UniProt: P90551
Ligands: MYS
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerol-3-phosphate dehydrogenase (EC 1.1.1.8)	protein	346	51% helix, 12% strand	P90551

Ligands and binding sites

MYS · Pentadecane · ligand · chains A

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

Pockets

3 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	645	0.70	0.78	48	empty
2	186	0.61	0.82	28	MYS
3	60	0.31	0.75	16	empty

Compared structures

1EVY · Crystal structure of leishmania mexicana glycerol-3-phosphate dehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00
P90551 · AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(+)]… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P90551
Elsewhere: RCSB PDB 1EVY · PDBe 1EVY · UniProt P90551

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