MolNFT v1 · #22293 · protein

Phosphoglucose isomerase from leishmania mexicana in complex with substrate D-fructose-6-phosphate

1T10 · Glucose-6-phosphate isomerase: “Phosphoglucose isomerase from leishmania mexicana in complex with substrate D-fructose-6-phosphate”. X-ray diffraction, 1 ligand (F6P), 3 pockets (best druggability 0.57). MolNFT v1 #22293 on…

PDB: 1T10
Type: protein
Length: 556 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucose-6-phosphate isomerase
EC: 5.3.1.9
UniProt: P42861
Ligands: F6P
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucose-6-phosphate isomerase (EC 5.3.1.9)	protein	556	53% helix, 12% strand	P42861

Ligands and binding sites

F6P · 6-O-phosphono-beta-D-fructofuranose · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	298	0.57	0.77	36	F6P
2	78	0.37	0.77	13	empty
3	82	0.37	0.77	14	empty

Compared structures

1T10 · Phosphoglucose isomerase from Leishmania mexicana in complex with substrate… · the same entry in another collection · chain A against A, TM-score 1.00
P42861 · AlphaFold monomer V2.0 prediction for glucose-6-phosphate isomerase (P42861) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P42861
Elsewhere: RCSB PDB 1T10 · PDBe 1T10 · UniProt P42861

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