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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
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0061621biological_processcanonical glycolysis
B0003824molecular_functioncatalytic activity
B0004619molecular_functionphosphoglycerate mutase activity
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016853molecular_functionisomerase activity
B0016868molecular_functionintramolecular phosphotransferase activity
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0061621biological_processcanonical glycolysis
C0003824molecular_functioncatalytic activity
C0004619molecular_functionphosphoglycerate mutase activity
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006094biological_processgluconeogenesis
C0006096biological_processglycolytic process
C0016853molecular_functionisomerase activity
C0016868molecular_functionintramolecular phosphotransferase activity
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0061621biological_processcanonical glycolysis
D0003824molecular_functioncatalytic activity
D0004619molecular_functionphosphoglycerate mutase activity
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006094biological_processgluconeogenesis
D0006096biological_processglycolytic process
D0016853molecular_functionisomerase activity
D0016868molecular_functionintramolecular phosphotransferase activity
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0061621biological_processcanonical glycolysis
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
DetailsActive site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15735341","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

247947

PDB entries from 2026-01-21

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