1E59

E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004619	molecular_function	phosphoglycerate mutase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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	0042803	molecular_function	protein homodimerization activity
A	0046538	molecular_function	2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
A	0061621	biological_process	canonical glycolysis
A	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A3001

Chain	Residue
A	TRP67
A	LYS82

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE VO3 A1001

Chain	Residue
A	ARG89
A	TYR91
A	LYS99
A	ARG115
A	ARG116
A	ASN185
A	HOH2009
A	HOH2114
A	HOH2115
A	HOH2116
A	HOH2262
A	HOH2263
A	ARG9
A	ASN16
A	ARG20
A	PHE21
A	THR22
A	GLY23
A	GLU88

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU7-ASN16

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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, ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145

Chain	Residue	Details
A	GLY11

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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, ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145

Chain	Residue	Details
A	ARG89

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:11884145

Chain	Residue	Details
A	HIS10
A	ARG89
A	ALA100
A	ASN185

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:11038361, ECO:0000269|PubMed:11884145

Chain	Residue	Details
A	GLY23
A	ARG116

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q3JWH7, ECO:0000255|HAMAP-Rule:MF_01039

Chain	Residue	Details
A	ALA62

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site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:11038361

Chain	Residue	Details
A	GLY184

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site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842

Chain	Residue	Details
A	GLU18
A	ALA100
A	TYR106

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qhf

Chain	Residue	Details
A	ARG61
A	HIS10
A	HIS183
A	GLU88

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