4EO9

Crystal structure of a phosphoglycerate mutase gpm1 from Mycobacterium leprae

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016853	molecular_function	isomerase activity
A	0016868	molecular_function	intramolecular phosphotransferase activity
A	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 301

Chain	Residue
A	LEU33
A	THR68

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Functional Information from PROSITE/UniProt

site_id	PS00175
Number of Residues	10
Details	PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LlRHGEsDwN

Chain	Residue	Details
A	LEU11-ASN20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	HIS14

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	GLU92

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site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	ARG65
A	GLU92
A	LYS103
A	ARG119
A	GLY186
A	ARG13
A	THR26

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	HIS185

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