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3IA3

A cis-proline in alpha-hemoglobin stabilizing Protein directs the structural reorganization of alpha-hemoglobin

Functional Information from GO Data
ChainGOidnamespacecontents
A0006457biological_processprotein folding
A0030218biological_processerythrocyte differentiation
A0030492molecular_functionhemoglobin binding
A0050821biological_processprotein stabilization
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005829cellular_componentcytosol
B0005833cellular_componenthemoglobin complex
B0015670biological_processcarbon dioxide transport
B0015671biological_processoxygen transport
B0016020cellular_componentmembrane
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030185biological_processnitric oxide transport
B0031720molecular_functionhaptoglobin binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042542biological_processresponse to hydrogen peroxide
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0071682cellular_componentendocytic vesicle lumen
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
C0006457biological_processprotein folding
C0030218biological_processerythrocyte differentiation
C0030492molecular_functionhemoglobin binding
C0050821biological_processprotein stabilization
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005829cellular_componentcytosol
D0005833cellular_componenthemoglobin complex
D0015670biological_processcarbon dioxide transport
D0015671biological_processoxygen transport
D0016020cellular_componentmembrane
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0030185biological_processnitric oxide transport
D0031720molecular_functionhaptoglobin binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042542biological_processresponse to hydrogen peroxide
D0042744biological_processhydrogen peroxide catabolic process
D0043177molecular_functionorganic acid binding
D0046872molecular_functionmetal ion binding
D0070062cellular_componentextracellular exosome
D0071682cellular_componentendocytic vesicle lumen
D0072562cellular_componentblood microparticle
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 201
ChainResidue
BPHE43
BVAL93
BASN97
BPHE98
BLEU101
BSER102
DPRO77
DASN78
DALA79
BHIS45
BPHE46
BHIS58
BLYS61
BVAL62
BALA65
BLEU83
BHIS87

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM D 201
ChainResidue
BMET76
BPRO77
BASN78
BALA79
DPHE43
DHIS45
DPHE46
DHIS58
DLYS61
DVAL62
DALA65
DLEU83
DHIS87
DVAL93
DASN97
DPHE98
DLEU101
DSER102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
BHIS58
DHIS58

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
BHIS87
DHIS87

site_idSWS_FT_FI3
Number of Residues28
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
BTHR8
BLEU91
BLEU106
BTHR108
BVAL121
BSER133
DTHR8
DALA13
DTYR24
DLEU29
DHIS45
BALA13
DASP47
DSER52
DVAL55
DGLY59
DLEU91
DLEU106
DTHR108
DVAL121
DSER133
BTYR24
BLEU29
BHIS45
BASP47
BSER52
BVAL55
BGLY59

site_idSWS_FT_FI4
Number of Residues10
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
BLYS11
DLYS99
BLYS56
BLYS60
BLYS90
BLYS99
DLYS11
DLYS56
DLYS60
DLYS90

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER3
BSER35
BSER49
DSER3
DSER35
DSER49

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BLYS7
BLYS16
BLYS40
DLYS7
DLYS16
DLYS40

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR8
DTHR8

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BLYS11
DLYS11

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTYR24
DTYR24

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BSER102
BSER124
BSER131
BSER138
DSER102
DSER124
DSER131
DSER138

site_idSWS_FT_FI11
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BTHR108
BTHR134
BTHR137
DTHR108
DTHR134
DTHR137

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
BLYS7
BLYS16
BLYS40
DLYS7
DLYS16
DLYS40

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
BLYS61
DLYS61

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PDB entries from 2024-07-31

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