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1RKD

E. COLI RIBOKINASE COMPLEXED WITH RIBOSE AND ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004747molecular_functionribokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019303biological_processD-ribose catabolic process
A0042803molecular_functionprotein homodimerization activity
A0044281biological_processsmall molecule metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAB1
Number of Residues4
DetailsRESIDUES MAKING DIRECT HYDROGEN BONDS WITH ADP.
ChainResidue
AASN187
ATHR223
AGLY225
AALA280

site_idAB2
Number of Residues7
DetailsRESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH ADP.
ChainResidue
AASN166
AASN187
AGLU190
ATHR223
APHE243
AVAL245
AALA280

site_idAB3
Number of Residues5
DetailsRESIDUES WITHIN VAN DER WAALS DISTANCE OF ADP.
ChainResidue
AGLY225
AVAL245
AALA253
AALA282
AVAL286

site_idRB1
Number of Residues7
DetailsRESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
ChainResidue
AASN14
AASP16
AGLY42
ALYS43
AASN46
AGLU143
AASP255

site_idRB2
Number of Residues3
DetailsRESIDUES MAKING WATER-MEDIATED HYDROGEN BONDS WITH RIBOSE.
ChainResidue
AASP255
AALA252
AGLY254

site_idRB3
Number of Residues5
DetailsRESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
ChainResidue
AALA98
AILE100
AILE110
AILE112
AILE251

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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11786021","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10438599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11786021","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9519409","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11786021","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01987","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10438599","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11786021","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

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

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PDB entries from 2025-10-01

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