MolNFT v1 · #92361 · protein

X-ray crystal structure of prostaglandin F synthase from leishmania major friedlin bound to NADPH

4G5D · Prostaglandin F2-alpha SYNTHASE/D-arabinose dehydrogenase: “X-ray crystal structure of prostaglandin F synthase from leishmania major friedlin bound to NADPH”. X-ray diffraction, 1 ligand (NDP), 2 pockets (best druggability 0.64).…

PDB: 4G5D
Type: protein
Length: 565 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Prostaglandin F2-alpha SYNTHASE/D-arabinose dehydrogenase
EC: 1.1.1.188
UniProt: Q4Q646
Ligands: NDP
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Prostaglandin F2-alpha SYNTHASE/D-arabinose dehydrogenase (EC 1.1.1.188)	protein	283	44% helix, 16% strand	Q4Q646
B	Prostaglandin F2-alpha SYNTHASE/D-arabinose dehydrogenase (EC 1.1.1.188)	protein	282	44% helix, 16% strand	Q4Q646

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 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	214	0.64	0.83	35	NDP
2	218	0.63	0.82	37	NDP

Interfaces

1 interface between chains.

A–B · 164 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4G5D · X-ray crystal structure of Prostaglandin f synthase from Leishmania major Friedlin bound… · 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 Q4Q646
Elsewhere: RCSB PDB 4G5D · PDBe 4G5D · UniProt Q4Q646

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