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6ZMY

Crystal structure of hemoglobin from turkey (Meleagiris gallopova) crystallized in monoclinic form at 1.66 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
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
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
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
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue HEM A 201
ChainResidue
ATYR42
AASN97
APHE98
ALEU101
ALEU136
AHOH302
AHOH304
AHOH352
AHOH356
AHOH369
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues13
Detailsbinding site for residue HEM B 201
ChainResidue
BPHE41
BPHE42
BHIS63
BSER70
BLEU88
BHIS92
BLEU96
BASN102
BPHE103
BLEU106
BLEU141
BHOH325
BHOH328

site_idAC3
Number of Residues17
Detailsbinding site for residue HEM C 201
ChainResidue
CTYR42
CPHE43
CHIS45
CHIS58
CLYS61
CLEU83
CHIS87
CLEU91
CASN97
CPHE98
CLEU101
CLEU136
CHOH303
CHOH309
CHOH311
CHOH326
CHOH338

site_idAC4
Number of Residues14
Detailsbinding site for residue HEM D 201
ChainResidue
DPHE41
DPHE42
DHIS63
DLYS66
DSER70
DPHE71
DLEU88
DHIS92
DLEU96
DASN102
DLEU106
DLEU141
DHOH323
DHOH344

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS58
CHIS58

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS87
CHIS87

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PDB entries from 2024-05-29

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