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5BYE

Crystal structure of human ribokinase in P212121 spacegroup

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004747molecular_functionribokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006014biological_processD-ribose metabolic process
A0006098biological_processpentose-phosphate shunt
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019303biological_processD-ribose catabolic process
A0042802molecular_functionidentical protein binding
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0004747molecular_functionribokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006014biological_processD-ribose metabolic process
B0006098biological_processpentose-phosphate shunt
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019303biological_processD-ribose catabolic process
B0042802molecular_functionidentical protein binding
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 401
ChainResidue
AASP263
ASER301
AALA304
ASER310
AHOH602
AHOH622

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 402
ChainResidue
AARG169
AHOH657
BARG34

site_idAC3
Number of Residues4
Detailsbinding site for residue NA B 401
ChainResidue
BSER301
BALA304
BGLY306
BSER310

Functional Information from PROSITE/UniProt
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDsfvGALA
ChainResidueDetails
AASP263-ALA276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues19
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A9J6","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03215","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JAN-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of human ribokinase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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