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3GYS

Crystal structure determination of cat (Felis silvestris catus) hemoglobin at 2.9 angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005833cellular_componenthemoglobin complex
A0015671biological_processoxygen transport
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0031838cellular_componenthaptoglobin-hemoglobin complex
A0046872molecular_functionmetal ion binding
A0048821biological_processerythrocyte development
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0046872molecular_functionmetal ion binding
B0048821biological_processerythrocyte development
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005833cellular_componenthemoglobin complex
C0015671biological_processoxygen transport
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0046872molecular_functionmetal ion binding
C0048821biological_processerythrocyte development
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0031721molecular_functionhemoglobin alpha binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0046872molecular_functionmetal ion binding
D0048821biological_processerythrocyte development
E0005344molecular_functionoxygen carrier activity
E0005506molecular_functioniron ion binding
E0005833cellular_componenthemoglobin complex
E0015671biological_processoxygen transport
E0019825molecular_functionoxygen binding
E0020037molecular_functionheme binding
E0031838cellular_componenthaptoglobin-hemoglobin complex
E0046872molecular_functionmetal ion binding
E0048821biological_processerythrocyte development
F0005344molecular_functionoxygen carrier activity
F0005833cellular_componenthemoglobin complex
F0015671biological_processoxygen transport
F0019825molecular_functionoxygen binding
F0020037molecular_functionheme binding
F0031721molecular_functionhemoglobin alpha binding
F0031838cellular_componenthaptoglobin-hemoglobin complex
F0046872molecular_functionmetal ion binding
F0048821biological_processerythrocyte development
G0005344molecular_functionoxygen carrier activity
G0005506molecular_functioniron ion binding
G0005833cellular_componenthemoglobin complex
G0015671biological_processoxygen transport
G0019825molecular_functionoxygen binding
G0020037molecular_functionheme binding
G0031838cellular_componenthaptoglobin-hemoglobin complex
G0046872molecular_functionmetal ion binding
G0048821biological_processerythrocyte development
H0005344molecular_functionoxygen carrier activity
H0005833cellular_componenthemoglobin complex
H0015671biological_processoxygen transport
H0019825molecular_functionoxygen binding
H0020037molecular_functionheme binding
H0031721molecular_functionhemoglobin alpha binding
H0031838cellular_componenthaptoglobin-hemoglobin complex
H0046872molecular_functionmetal ion binding
H0048821biological_processerythrocyte development
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 143
ChainResidue
ATYR42
AASN97
APHE98
ALEU101
ALEU136
AHOH142
APHE43
AHIS45
AHIS58
ALYS61
ALEU86
AHIS87
ALEU91
AVAL93

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEM B 148
ChainResidue
BPHE41
BPHE42
BHIS63
BHIS92
BLEU96
BASN102
BPHE103
BLEU106
BLEU141

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM C 143
ChainResidue
CTYR42
CPHE43
CHIS45
CPHE46
CHIS58
CLYS61
CALA65
CLEU86
CHIS87
CLEU91
CVAL93
CPHE98
CLEU101
CHOH142

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM D 148
ChainResidue
DPHE41
DPHE42
DHIS63
DLYS66
DVAL67
DSER70
DLEU88
DHIS92
DLEU96
DASN102
DLEU106
DLEU141

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM E 143
ChainResidue
ETYR42
EPHE43
EHIS45
EPHE46
EHIS58
ELYS61
EALA65
ELEU83
EHIS87
EVAL93
EASN97
EPHE98
ELEU101
EHOH142

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM F 148
ChainResidue
FTHR38
FPHE41
FPHE42
FHIS63
FLYS66
FHIS92
FLEU96
FVAL98
FASN102
FLEU106
FLEU141
FHOH147

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM G 143
ChainResidue
GTYR42
GPHE43
GHIS45
GPHE46
GLYS61
GVAL62
GLEU83
GHIS87
GLEU91
GVAL93
GASN97
GPHE98
GLEU101
GLEU136
GHOH144

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM H 148
ChainResidue
HASN102
HPHE103
HLEU106
HLEU141
HTHR38
HPHE41
HPHE42
HHIS63
HSER70
HLEU88
HLEU91
HHIS92
HLEU96

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsPeptide: {"description":"Hemopressin","featureId":"PRO_0000455877","evidences":[{"source":"UniProtKB","id":"P01946","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P69905","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P01942","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues576
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P68871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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