2DKA

Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, in the apo-form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004610	molecular_function	phosphoacetylglucosamine mutase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0030097	biological_process	hemopoiesis
A	0034221	biological_process	fungal-type cell wall chitin biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization
A	0071704	biological_process	organic substance metabolic process
B	0000287	molecular_function	magnesium ion binding
B	0004610	molecular_function	phosphoacetylglucosamine mutase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0006048	biological_process	UDP-N-acetylglucosamine biosynthetic process
B	0016853	molecular_function	isomerase activity
B	0016868	molecular_function	intramolecular phosphotransferase activity
B	0030097	biological_process	hemopoiesis
B	0034221	biological_process	fungal-type cell wall chitin biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
B	0071704	biological_process	organic substance metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00710
Number of Residues	10
Details	PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmITASHNP

Chain	Residue	Details
A	GLY60-PRO69

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Phosphoserine intermediate => ECO:0000305\|PubMed:16651269

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: via phosphate group => ECO:0000305\|PubMed:16651269