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2QSP

Bovine Hemoglobin at pH 5.7

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein 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
C0005515molecular_functionprotein 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
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
APHE98
ALEU101
ALEU136
AHOH222
AHOH306
AHOH316
APHE43
APHE46
AHIS58
ALYS61
ALEU86
AHIS87
ALEU91
AASN97

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 146
ChainResidue
BTHR37
BPHE40
BPHE41
BHIS62
BLYS65
BLEU90
BHIS91
BLEU95
BASN101
BPHE102
BLEU105
BLEU140
BHOH164
BHOH262
DLYS7
DHOH238

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM C 142
ChainResidue
CTYR42
CPHE43
CHIS45
CHIS58
CLYS61
CLEU83
CHIS87
CLEU91
CASN97
CPHE98
CLEU101
CLEU136
CHOH374
CHOH397
CHOH417
CHOH426

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM D 146
ChainResidue
CALA4
DTHR37
DPHE40
DPHE41
DHIS62
DLYS65
DSER69
DHIS91
DLEU95
DASN101
DLEU140
DHOH153
DHOH168
DHOH178
DHOH210
DHOH222
DHOH236
DHOH262
DHOH324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue
ChainResidueDetails
BHIS62
DHIS62

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue
ChainResidueDetails
BHIS91
DHIS91

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BTHR11
DTHR11
ASER49
CSER3
CSER35
CSER49

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BSER43
DSER43
ALYS40
CLYS7
CLYS11
CLYS40

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BLYS58
BLYS81
DLYS58
DLYS81

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BCYS92
DCYS92

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ASER102
ASER124
ASER138
CSER102
CSER124
CSER138

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR108
ATHR134
ATHR137
CTHR108
CTHR134
CTHR137

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PDB entries from 2025-07-02

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