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1RII

Crystal structure of phosphoglycerate mutase from M. Tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004619molecular_functionphosphoglycerate mutase activity
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
C0003824molecular_functioncatalytic activity
C0004619molecular_functionphosphoglycerate mutase activity
C0005886cellular_componentplasma membrane
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0016868molecular_functionintramolecular phosphotransferase activity
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
D0003824molecular_functioncatalytic activity
D0004619molecular_functionphosphoglycerate mutase activity
D0005886cellular_componentplasma membrane
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0016868molecular_functionintramolecular phosphotransferase activity
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0046538molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 501
ChainResidue
AHIS12
ASER15
AASN18
ATHR24
AARG63
AGLU90
AHOH622

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BASN18
BTHR24
BARG63
BGLU90
BHIS183
BHOH607
BHOH1001
BHIS12
BSER15

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 503
ChainResidue
DHIS12
DSER15
DASN18
DTHR24
DARG63
DGLU90
DHIS183
DHOH636
DHOH814

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL D 504
ChainResidue
DGLN132
DHOH939

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL D 505
ChainResidue
CARG83
DTYR57
DARG83
DVAL167
DHOH888

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LlRHGEsDwN
ChainResidueDetails
ALEU9-ASN18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS12
BHIS12
CHIS12
DHIS12

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AGLU90
BGLU90
CGLU90
DGLU90

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:15735341
ChainResidueDetails
AARG11
CTHR24
CARG63
CGLU90
DARG11
DTHR24
DARG63
DGLU90
ATHR24
AARG63
AGLU90
BARG11
BTHR24
BARG63
BGLU90
CARG11

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
ALYS101
DLYS101
DARG117
DGLY184
AARG117
AGLY184
BLYS101
BARG117
BGLY184
CLYS101
CARG117
CGLY184

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01039
ChainResidueDetails
AHIS183
BHIS183
CHIS183
DHIS183

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
AGLU90
AHIS183
AARG63
AHIS12

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
BGLU90
BHIS183
BARG63
BHIS12

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
CGLU90
CHIS183
CARG63
CHIS12

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1qhf
ChainResidueDetails
DGLU90
DHIS183
DARG63
DHIS12

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PDB entries from 2024-07-24

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