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Crystal structure of X. citri phosphoglucomutase in complex with 1- methyl-glucose 6-phosphate

Analyse Crystal structure of X. citri phosphoglucomutase in complex with 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N1E
Type: protein
Length: 448 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE
UniProt: A0A2K2R2Z1
Ligands: QIF, MG
Pockets: 3 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE	protein	448	41% helix, 21% strand	A0A2K2R2Z1

Ligands and binding sites

QIF · 1-deoxy-7-O-phosphono-alpha-D-gluco-hept-2-ulopyranose · 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	523	0.74	0.82	56	QIF
2	60	0.33	0.77	14	empty
3	55	0.28	0.74	14	empty

Compared structures

6N1E · Crystal structure of X. citri phosphoglucomutase in complex with 1-methyl-glucose… · 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 A0A2K2R2Z1
Elsewhere: RCSB PDB 6N1E · PDBe 6N1E · UniProt A0A2K2R2Z1

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