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1GQT

Activation of Ribokinase by Monovalent Cations

Functional Information from GO Data
ChainGOidnamespacecontents
A0004747molecular_functionribokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0006796biological_processphosphate-containing compound metabolic process
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0019303biological_processD-ribose catabolic process
A0042803molecular_functionprotein homodimerization activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
B0004747molecular_functionribokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006014biological_processD-ribose metabolic process
B0006796biological_processphosphate-containing compound metabolic process
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0019303biological_processD-ribose catabolic process
B0042803molecular_functionprotein homodimerization activity
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
C0004747molecular_functionribokinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006014biological_processD-ribose metabolic process
C0006796biological_processphosphate-containing compound metabolic process
C0016301molecular_functionkinase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0019303biological_processD-ribose catabolic process
C0042803molecular_functionprotein homodimerization activity
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
D0004747molecular_functionribokinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006014biological_processD-ribose metabolic process
D0006796biological_processphosphate-containing compound metabolic process
D0016301molecular_functionkinase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0019303biological_processD-ribose catabolic process
D0042803molecular_functionprotein homodimerization activity
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTiAAGDtfnGALI
ChainResidueDetails
AASP249-ILE262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
ChainResidueDetails
AASP255
BASP255
CASP255
DASP255

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
ChainResidueDetails
AASN14
BGLU143
BASN187
BTHR223
BASP255
BHIS279
CASN14
CGLY42
CGLU143
CASN187
CTHR223
AGLY42
CASP255
CHIS279
DASN14
DGLY42
DGLU143
DASN187
DTHR223
DASP255
DHIS279
AGLU143
AASN187
ATHR223
AASP255
AHIS279
BASN14
BGLY42

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
ChainResidueDetails
AASP249
BARG288
BGLY290
BSER294
CASP249
CILE251
CALA285
CARG288
CGLY290
CSER294
DASP249
AILE251
DILE251
DALA285
DARG288
DGLY290
DSER294
AALA285
AARG288
AGLY290
ASER294
BASP249
BILE251
BALA285

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
ChainResidueDetails
AGLY254
BGLY254
CGLY254
DGLY254

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
AGLY254
AASP255
AALA253
AALA252

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
BGLY254
BASP255
BALA253
BALA252

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
CGLY254
CASP255
CALA253
CALA252

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rk2
ChainResidueDetails
DGLY254
DASP255
DALA253
DALA252

site_idMCSA1
Number of Residues4
DetailsM-CSA 663
ChainResidueDetails
AALA252electrostatic stabiliser, polar interaction
AALA253electrostatic stabiliser, polar interaction
AGLY254electrostatic stabiliser, polar interaction
AASP255electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 663
ChainResidueDetails
BALA252electrostatic stabiliser, polar interaction
BALA253electrostatic stabiliser, polar interaction
BGLY254electrostatic stabiliser, polar interaction
BASP255electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA3
Number of Residues4
DetailsM-CSA 663
ChainResidueDetails
CALA252electrostatic stabiliser, polar interaction
CALA253electrostatic stabiliser, polar interaction
CGLY254electrostatic stabiliser, polar interaction
CASP255electrostatic stabiliser, proton acceptor, proton donor

site_idMCSA4
Number of Residues4
DetailsM-CSA 663
ChainResidueDetails
DALA252electrostatic stabiliser, polar interaction
DALA253electrostatic stabiliser, polar interaction
DGLY254electrostatic stabiliser, polar interaction
DASP255electrostatic stabiliser, proton acceptor, proton donor

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PDB entries from 2024-06-26

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