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Crystal structure of a phosphoglycerate mutase GPM1 from mycobacterium leprae

Analyse Crystal structure of a phosphoglycerate mutase GPM1 from mycobacterium leprae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EO9
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
EC: 5.4.2.1
UniProt: B8ZT86
Ligands: CL
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (EC 5.4.2.1)	protein	240	45% helix, 12% strand	B8ZT86

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	329	0.60	0.78	35	empty

Compared structures

4EO9 · Crystal structure of a phosphoglycerate mutase gpm1 from Mycobacterium leprae · the same entry in another collection · chain A against A, TM-score 1.00
B8ZT86 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- dependent phosphoglycerate… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 B8ZT86
Elsewhere: RCSB PDB 4EO9 · PDBe 4EO9 · UniProt B8ZT86

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