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Crystal structure of X. citri phosphoglucomutase in complex with 2- fluoro mannosyl-1-methyl-phosphonic acid

Analyse Crystal structure of X. citri phosphoglucomutase in complex with 2- fluoro… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MLW
Type: protein
Length: 449 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoglucomutase
UniProt: Q8PGN7
Ligands: JVA, MG
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoglucomutase	protein	449	41% helix, 21% strand	Q8PGN7

Ligands and binding sites

JVA · 2,6-anhydro-5,7-dideoxy-5-fluoro-7-phosphono-D-glycero-D-manno-heptitol · ligand · chains A
MG · Magnesium ion · metal · 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	466	0.75	0.84	56	JVA
2	55	0.29	0.75	13	empty
3	56	0.29	0.75	14	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

6MLW · Crystal structure of X. citri phosphoglucomutase in complex with 2-fluoro… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8PGN7
Elsewhere: RCSB PDB 6MLW · PDBe 6MLW · UniProt Q8PGN7

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