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1HKC

RECOMBINANT HUMAN HEXOKINASE TYPE I COMPLEXED WITH GLUCOSE AND PHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0001678biological_processintracellular glucose homeostasis
A0002720biological_processpositive regulation of cytokine production involved in immune response
A0004340molecular_functionglucokinase activity
A0004396molecular_functionhexokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005536molecular_functionD-glucose binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006002biological_processfructose 6-phosphate metabolic process
A0006006biological_processglucose metabolic process
A0006013biological_processmannose metabolic process
A0006096biological_processglycolytic process
A0006954biological_processinflammatory response
A0008865molecular_functionfructokinase activity
A0009298biological_processGDP-mannose biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019158molecular_functionmannokinase activity
A0019318biological_processhexose metabolic process
A0032731biological_processpositive regulation of interleukin-1 beta production
A0042834molecular_functionpeptidoglycan binding
A0045087biological_processinnate immune response
A0045121cellular_componentmembrane raft
A0046835biological_processcarbohydrate phosphorylation
A0047931molecular_functionglucosamine kinase activity
A0051156biological_processglucose 6-phosphate metabolic process
A0061621biological_processcanonical glycolysis
A0061728biological_processGDP-mannose biosynthetic process from mannose
A0072655biological_processestablishment of protein localization to mitochondrion
A0072656biological_processmaintenance of protein location in mitochondrion
A0141199biological_processGDP-mannose biosynthetic process from glucose
A1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idGLN
Number of Residues7
DetailsGLUCOSE BINDING SITE IN N-TERMINAL DOMAIN.
ChainResidue
ATHR172
ALYS173
AASP209
AASN235
AGLU260
AGLN291
AGLU294

site_idMEC
Number of Residues4
DetailsMETAL ION BINDING SITE IN C-TERMINAL DOMAIN.
ChainResidue
AMET690
AVAL693
AVAL696
AGLY698

site_idMEN
Number of Residues4
DetailsMETAL ION BINDING SITE IN N-TERMINAL DOMAIN.
ChainResidue
ALEU242
AILE245
AVAL248
AGLY250

site_idPIC
Number of Residues2
DetailsPHOSPHATE BINDING SITE IN C-TERMINAL DOMAIN.
ChainResidue
ATHR680
ATHR863

site_idPIN
Number of Residues3
DetailsPHOSPHATE BINDING SITE IN N-TERMINAL DOMAIN.
ChainResidue
ASER415
ASER88
ATHR232

Functional Information from PROSITE/UniProt
site_idPS00378
Number of Residues26
DetailsHEXOKINASE_1 Hexokinase domain signature. VGFTFSFPcqqskIDeaiLitWTKrF
ChainResidueDetails
AVAL150-PHE175
ALEU598-PHE623

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1QHA
ChainResidueDetails
AARG30
AARG425

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKC
ChainResidueDetails
AASP84
ATHR863

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1HKC, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA
ChainResidueDetails
ASER155

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0000269|PubMed:9735292, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1HKC, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB
ChainResidueDetails
ATHR172
AASN208
AASN235
AGLU260
AGLN291

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA
ChainResidueDetails
AASP209

site_idSWS_FT_FI6
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB
ChainResidueDetails
ATHR232
AASP413
ASER449
ATHR680
AASP861

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0007744|PDB:1QHA
ChainResidueDetails
AASN345

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA
ChainResidueDetails
AASP532

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB
ChainResidueDetails
ASER603

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1DGK, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOE, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB
ChainResidueDetails
ATHR620
AASN656
ASER682
AGLU708
AGLU742

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA
ChainResidueDetails
AASP657

site_idSWS_FT_FI12
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10686099, ECO:0007744|PDB:1DGK
ChainResidueDetails
AGLY747
ATHR784

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10574795, ECO:0000269|PubMed:10686099, ECO:0000269|PubMed:9493266, ECO:0007744|PDB:1CZA, ECO:0007744|PDB:1HKB, ECO:0007744|PDB:1QHA, ECO:0007744|PDB:4F9O, ECO:0007744|PDB:4FOI, ECO:0007744|PDB:4FPA, ECO:0007744|PDB:4FPB
ChainResidueDetails
ASER897

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
AMET1

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05708
ChainResidueDetails
ASER337

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 696
ChainResidueDetails
AARG539electrostatic stabiliser, polar interaction
ASER603electrostatic stabiliser, polar interaction
AASP657proton acceptor, proton donor

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PDB entries from 2024-09-11

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