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6JJ8

Crystal structure of OsHXK6-ATP-Mg2+ complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001678biological_processintracellular glucose homeostasis
A0004340molecular_functionglucokinase activity
A0004396molecular_functionhexokinase activity
A0005524molecular_functionATP binding
A0005536molecular_functionD-glucose binding
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0006096biological_processglycolytic process
A0008865molecular_functionfructokinase activity
A0009707cellular_componentchloroplast outer membrane
A0009749biological_processresponse to glucose
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019318biological_processhexose metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0051156biological_processglucose 6-phosphate metabolic process
B0000166molecular_functionnucleotide binding
B0001678biological_processintracellular glucose homeostasis
B0004340molecular_functionglucokinase activity
B0004396molecular_functionhexokinase activity
B0005524molecular_functionATP binding
B0005536molecular_functionD-glucose binding
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0006096biological_processglycolytic process
B0008865molecular_functionfructokinase activity
B0009707cellular_componentchloroplast outer membrane
B0009749biological_processresponse to glucose
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0019318biological_processhexose metabolic process
B0046835biological_processcarbohydrate phosphorylation
B0051156biological_processglucose 6-phosphate metabolic process
C0000166molecular_functionnucleotide binding
C0001678biological_processintracellular glucose homeostasis
C0004340molecular_functionglucokinase activity
C0004396molecular_functionhexokinase activity
C0005524molecular_functionATP binding
C0005536molecular_functionD-glucose binding
C0005739cellular_componentmitochondrion
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0006006biological_processglucose metabolic process
C0006096biological_processglycolytic process
C0008865molecular_functionfructokinase activity
C0009707cellular_componentchloroplast outer membrane
C0009749biological_processresponse to glucose
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0019318biological_processhexose metabolic process
C0046835biological_processcarbohydrate phosphorylation
C0051156biological_processglucose 6-phosphate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue ADP C 601
ChainResidue
CGLY112
CGLY450
CGLY451
CLEU452
CHIS455
CPO4602
CMG603
CTHR113
CASN114
CGLY260
CTHR261
CGLY328
CTHR365
CPRO366
CSER369

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 C 602
ChainResidue
CASP109
CSER185
CASP238
CASP449
CASP486
CSER488
CADP601

site_idAC3
Number of Residues3
Detailsbinding site for residue MG C 603
ChainResidue
CGLU136
CASP486
CADP601

site_idAC4
Number of Residues13
Detailsbinding site for residue ADP A 601
ChainResidue
AGLY112
ATHR113
AASN114
ATHR261
AGLY328
APRO366
ASER369
AGLY450
AGLY451
ALEU452
AHIS455
APO4602
AMG603

site_idAC5
Number of Residues7
Detailsbinding site for residue PO4 A 602
ChainResidue
AASP109
ASER185
AASP238
AASP449
AASP486
ASER488
AADP601

site_idAC6
Number of Residues3
Detailsbinding site for residue MG A 603
ChainResidue
AGLU136
AASP486
AADP601

site_idAC7
Number of Residues13
Detailsbinding site for residue ADP B 601
ChainResidue
BGLY112
BTHR113
BASN114
BGLY260
BTHR261
BGLY328
BSER369
BGLY450
BGLY451
BLEU452
BHIS455
BPO4602
BMG603

site_idAC8
Number of Residues7
Detailsbinding site for residue PO4 B 602
ChainResidue
BASP109
BSER185
BASP238
BASP449
BASP486
BSER488
BADP601

site_idAC9
Number of Residues2
Detailsbinding site for residue MG B 603
ChainResidue
BASP486
BADP601

Functional Information from PROSITE/UniProt
site_idPS00378
Number of Residues26
DetailsHEXOKINASE_1 Hexokinase domain signature. LGFTFSFPvhqtsISsgtLikWTKgF
ChainResidueDetails
CLEU180-PHE205

site_idPS00782
Number of Residues16
DetailsTFIIB Transcription factor TFIIB repeat signature. GRyvdNDVAAAVILGT
ChainResidueDetails
CGLY246-THR261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1362
DetailsDomain: {"description":"Hexokinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues414
DetailsRegion: {"description":"Hexokinase small subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues747
DetailsRegion: {"description":"Hexokinase large subdomain","evidences":[{"source":"PROSITE-ProRule","id":"PRU01084","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31176485","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JJ8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JJ9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31176485","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JJ8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31176485","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2018","submissionDatabase":"PDB data bank","title":"Crystal structure of Oryza sativa hexokinase 6.","authors":["Matsudaira K.","Mochizuki S.","Yoshida H.","Kamitori S.","Akimitsu K."]}},{"source":"PDB","id":"5ZQT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JJ7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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