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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1HDS

MACROMOLECULAR STRUCTURE REFINEMENT BY RESTRAINED LEAST-SQUARES AND INTERACTIVE GRAPHICS AS APPLIED TO SICKLING DEER TYPE III HEMOGLOBIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031720molecular_functionhaptoglobin binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0042744biological_processhydrogen peroxide catabolic process
A0043177molecular_functionorganic acid binding
A0046872molecular_functionmetal ion binding
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005833cellular_componenthemoglobin complex
C0015671biological_processoxygen transport
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0031720molecular_functionhaptoglobin binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0042744biological_processhydrogen peroxide catabolic process
C0043177molecular_functionorganic acid binding
C0046872molecular_functionmetal ion binding
C0072562cellular_componentblood microparticle
C0098869biological_processcellular oxidant detoxification
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0031720molecular_functionhaptoglobin binding
D0031721molecular_functionhemoglobin alpha binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042744biological_processhydrogen peroxide catabolic process
D0043177molecular_functionorganic acid binding
D0046872molecular_functionmetal ion binding
D0072562cellular_componentblood microparticle
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATHR39
AVAL93
AASN97
ALEU136
ATYR42
APHE43
AHIS58
ALYS61
AVAL62
ALEU86
AHIS87
ALEU91
site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HEM B 146
ChainResidue
BPHE40
BHIS43
BHIS62
BARG65
BPHE84
BHIS91
BLEU95
BVAL97
BASN101
BPHE102
BLEU105
site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM C 142
ChainResidue
CTHR39
CTYR42
CPHE43
CHIS45
CHIS58
CLEU83
CLEU86
CHIS87
CLEU91
CVAL93
CASN97
CLEU101
CASP132
site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HEM D 146
ChainResidue
DPHE40
DHIS43
DHIS62
DVAL66
DHIS91
DLYS94
DLEU95
DASN101
DPHE102
DLEU105
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues568
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"description":"distal binding residue","evidences":[{"source":"UniProtKB","id":"P80044","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1977","firstPage":"335","lastPage":"342","volume":"33","journal":"Acta Crystallogr. B","title":"The structure of sickling deer type III hemoglobin by molecular replacement.","authors":["Schmidt W.C. Jr.","Girling R.L.","Houston T.E.","Sproul G.D.","Amma E.L.","Huisman T.H.J."]}},{"source":"PDB","id":"1HDS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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