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X-ray crystal structure of PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE family protein (BTH_I1489)FROM burkholderia thailandensis

Analyse X-ray crystal structure of PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE family protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UW2
Type: protein
Length: 458 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE family protein
UniProt: Q2SYG4
Ligands: ZN, PO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PHOSPHOGLUCOMUTASE/PHOSPHOMANNOMUTASE family protein	protein	458	36% helix, 23% strand	Q2SYG4

Ligands and binding sites

ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 6 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

2 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	696	0.74	0.80	72	PO4, EDO, GOL
2	77	0.41	0.79	18	empty

Compared structures

3UW2 · X-ray Crystal Structure of Phosphoglucomutase/phosphomannomutase family protein… · 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 Q2SYG4
Elsewhere: RCSB PDB 3UW2 · PDBe 3UW2 · UniProt Q2SYG4

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