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5EE4

The crystal structure of HpuA from Kingella denitrificans in complex with human haemoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0009279cellular_componentcell outer membrane
B0009279cellular_componentcell outer membrane
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005829cellular_componentcytosol
C0005833cellular_componenthemoglobin complex
C0006954biological_processinflammatory response
C0015670biological_processcarbon dioxide transport
C0015671biological_processoxygen transport
C0016020cellular_componentmembrane
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0030185biological_processnitric oxide transport
C0031720molecular_functionhaptoglobin binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0042542biological_processresponse to hydrogen peroxide
C0042744biological_processhydrogen peroxide catabolic process
C0046872molecular_functionmetal ion binding
C0048821biological_processerythrocyte development
C0070062cellular_componentextracellular exosome
C0071682cellular_componentendocytic vesicle lumen
C0072562cellular_componentblood microparticle
C0098869biological_processcellular oxidant detoxification
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005829cellular_componentcytosol
D0005833cellular_componenthemoglobin complex
D0006954biological_processinflammatory response
D0008217biological_processregulation of blood pressure
D0015670biological_processcarbon dioxide transport
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0030185biological_processnitric oxide transport
D0030492molecular_functionhemoglobin binding
D0031720molecular_functionhaptoglobin binding
D0031721molecular_functionhemoglobin alpha binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042542biological_processresponse to hydrogen peroxide
D0042744biological_processhydrogen peroxide catabolic process
D0045429biological_processpositive regulation of nitric oxide biosynthetic process
D0046872molecular_functionmetal ion binding
D0048821biological_processerythrocyte development
D0070062cellular_componentextracellular exosome
D0070293biological_processrenal absorption
D0070527biological_processplatelet aggregation
D0071682cellular_componentendocytic vesicle lumen
D0072562cellular_componentblood microparticle
D0097746biological_processblood vessel diameter maintenance
D0098869biological_processcellular oxidant detoxification
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
E0004601molecular_functionperoxidase activity
E0005344molecular_functionoxygen carrier activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005829cellular_componentcytosol
E0005833cellular_componenthemoglobin complex
E0006954biological_processinflammatory response
E0015670biological_processcarbon dioxide transport
E0015671biological_processoxygen transport
E0016020cellular_componentmembrane
E0019825molecular_functionoxygen binding
E0020037molecular_functionheme binding
E0030185biological_processnitric oxide transport
E0031720molecular_functionhaptoglobin binding
E0031838cellular_componenthaptoglobin-hemoglobin complex
E0042542biological_processresponse to hydrogen peroxide
E0042744biological_processhydrogen peroxide catabolic process
E0046872molecular_functionmetal ion binding
E0048821biological_processerythrocyte development
E0070062cellular_componentextracellular exosome
E0071682cellular_componentendocytic vesicle lumen
E0072562cellular_componentblood microparticle
E0098869biological_processcellular oxidant detoxification
F0004601molecular_functionperoxidase activity
F0005344molecular_functionoxygen carrier activity
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005615cellular_componentextracellular space
F0005829cellular_componentcytosol
F0005833cellular_componenthemoglobin complex
F0006954biological_processinflammatory response
F0008217biological_processregulation of blood pressure
F0015670biological_processcarbon dioxide transport
F0015671biological_processoxygen transport
F0019825molecular_functionoxygen binding
F0020037molecular_functionheme binding
F0030185biological_processnitric oxide transport
F0030492molecular_functionhemoglobin binding
F0031720molecular_functionhaptoglobin binding
F0031721molecular_functionhemoglobin alpha binding
F0031838cellular_componenthaptoglobin-hemoglobin complex
F0042542biological_processresponse to hydrogen peroxide
F0042744biological_processhydrogen peroxide catabolic process
F0045429biological_processpositive regulation of nitric oxide biosynthetic process
F0046872molecular_functionmetal ion binding
F0048821biological_processerythrocyte development
F0070062cellular_componentextracellular exosome
F0070293biological_processrenal absorption
F0070527biological_processplatelet aggregation
F0071682cellular_componentendocytic vesicle lumen
F0072562cellular_componentblood microparticle
F0097746biological_processblood vessel diameter maintenance
F0098869biological_processcellular oxidant detoxification
F1904724cellular_componenttertiary granule lumen
F1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GOL A 401
ChainResidue
AGLU269
AHIS278
AGLY282
AARG304

site_idAC2
Number of Residues13
Detailsbinding site for residue HEM C 201
ChainResidue
CLEU86
CHIS87
CLEU91
CASN97
CPHE98
COXY202
CHOH306
CHOH327
CTYR42
CPHE43
CPHE46
CHIS58
CLEU83

site_idAC3
Number of Residues3
Detailsbinding site for residue OXY C 202
ChainResidue
CHIS58
CVAL62
CHEM201

site_idAC4
Number of Residues11
Detailsbinding site for residue HEM D 201
ChainResidue
DPHE41
DPHE42
DHIS63
DLEU88
DHIS92
DLEU96
DASN102
DLEU106
DVAL137
DLEU141
DOXY202

site_idAC5
Number of Residues3
Detailsbinding site for residue OXY D 202
ChainResidue
DHIS63
DVAL67
DHEM201

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL D 203
ChainResidue
DVAL1
DLEU78
DASP79
DASN80
DLEU81
DLYS82

site_idAC7
Number of Residues14
Detailsbinding site for residue HEM E 201
ChainResidue
ETYR42
EPHE43
EHIS58
ELYS61
ELEU83
EHIS87
ELEU91
EASN97
EPHE98
ELEU101
ELEU136
EOXY202
EHOH320
EHOH339

site_idAC8
Number of Residues3
Detailsbinding site for residue OXY E 202
ChainResidue
EHIS58
EVAL62
EHEM201

site_idAC9
Number of Residues13
Detailsbinding site for residue HEM F 201
ChainResidue
FPHE41
FPHE42
FHIS63
FPHE71
FLEU88
FLEU91
FHIS92
FLEU96
FASN102
FLEU106
FVAL137
FLEU141
FOXY202

site_idAD1
Number of Residues3
Detailsbinding site for residue OXY F 202
ChainResidue
FHIS63
FVAL67
FHEM201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsPeptide: {"description":"Hemopressin","featureId":"PRO_0000455882","evidences":[{"source":"PubMed","id":"18077343","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues424
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues66
DetailsSite: {"description":"(Microbial infection) Cleavage; by N.americanus apr-2","evidences":[{"source":"PubMed","id":"12552433","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsSite: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; alternate","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"7358733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues18
DetailsPeptide: {"description":"LVV-hemorphin-7","featureId":"PRO_0000296641"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues12
DetailsPeptide: {"description":"Spinorphin","featureId":"PRO_0000424226"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N-pyruvate 2-iminyl-valine; in Hb A1b"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"8637569","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9843411","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"4531009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) valine; in Hb A1c","evidences":[{"source":"PubMed","id":"635569","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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