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3PIA

Site-specific Glycosylation of Hemoglobin Utilizing Oxime Ligation Chemistry as a Viable Alternative to PEGylation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein 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
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
B0098869biological_processcellular oxidant detoxification
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein 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
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
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
AASN97
APHE98
ALEU101
AVAL132
ALEU136
ACMO143
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 143
ChainResidue
AHIS58
AVAL62
AHEM142

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BTHR38
BPHE41
BPHE42
BHIS63
BSER70
BPHE71
BLEU91
BHIS92
BLEU96
BASN102
BLEU106
BVAL137
BLEU141
BCMO148

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BHIS63
BVAL67
BHEM147

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM C 142
ChainResidue
AALA12
ALYS16
CTYR42
CPHE43
CHIS45
CHIS58
CLYS61
CLEU83
CLEU86
CHIS87
CLEU91
CVAL93
CASN97
CPHE98
CLEU101
CCMO143
CHOH202
CHOH210

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO C 143
ChainResidue
CHIS58
CVAL62
CHEM142

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM D 147
ChainResidue
DTHR38
DPHE41
DPHE42
DPHE45
DHIS63
DSER70
DPHE71
DHIS92
DLEU96
DASN102
DPHE103
DLEU141
DCMO148

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO D 148
ChainResidue
DHIS63
DVAL67
DHEM147

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

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ASER3
ASER35
ASER49
CSER3
CSER35
CSER49

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALYS7
ALYS11
ALYS40
CLYS7
CLYS11
CLYS40

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALYS16
CLYS16
DLYS59
DLYS82

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ATYR24
CTYR24

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 2024-07-17

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