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4EMB

Crystal structure of a phosphoglycerate mutase gpmA from Borrelia burgdorferi B31

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005829cellular_componentcytosol
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
C0003824molecular_functioncatalytic activity
C0004619molecular_functionphosphoglycerate mutase activity
C0005829cellular_componentcytosol
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0016868molecular_functionintramolecular phosphotransferase activity
C0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
D0003824molecular_functioncatalytic activity
D0004619molecular_functionphosphoglycerate mutase activity
D0005829cellular_componentcytosol
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0016868molecular_functionintramolecular phosphotransferase activity
D0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
ALEU24
APHE25
ATHR26
AGLY27
AGLU92
ATYR95

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
BGLU92
BTYR95
BPHE25
BTHR26
BGLY27

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 301
ChainResidue
CLEU24
CPHE25
CTHR26
CGLY27
CGLU92
CTYR95

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGEsEwN
ChainResidueDetails
ALEU11-ASN20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS14
BHIS14
CHIS14
DHIS14

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AGLU92
BGLU92
CGLU92
DGLU92

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
BTHR26
BARG65
BGLU92
BLYS103
BARG119
BGLY188
CARG13
CTHR26
CARG65
CGLU92
CLYS103
CARG119
CGLY188
DARG13
DTHR26
DARG65
DGLU92
DLYS103
DARG119
DGLY188
AARG13
ATHR26
AARG65
AGLU92
ALYS103
AARG119
AGLY188
BARG13

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS187
BHIS187
CHIS187
DHIS187

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PDB entries from 2024-05-29

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