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1RKS

E. COLI RIBOKINASE IN COMPLEX WITH D-RIBOSE

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
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0019303biological_processD-ribose catabolic process
A0042803molecular_functionprotein homodimerization activity
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idRB1
Number of Residues7
DetailsRESIDUES MAKING DIRECT HYDROGEN BONDS WITH RIBOSE.
ChainResidue
AASN14
AASP16
AGLY42
ALYS43
AASN46
AGLU143
AASP255

site_idRB2
Number of Residues5
DetailsRESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.
ChainResidue
AILE110
AILE112
AILE251
AALA98
AILE100

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
ChainResidueDetails
AASP255

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021, ECO:0000269|PubMed:9519409
ChainResidueDetails
AGLY42
AGLU143
AASN187
ATHR223
AASP255
AHIS279
AASN14

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000305|PubMed:11786021
ChainResidueDetails
AILE251
AALA285
AARG288
AGLY290
ASER294
AASP249

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021
ChainResidueDetails
AGLY254

Catalytic Information from CSA
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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数据于2024-04-17公开中

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