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1Z8U

Crystal structure of oxidized alpha hemoglobin bound to AHSP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005833cellular_componenthemoglobin complex
A0006457biological_processprotein folding
A0020027biological_processhemoglobin metabolic process
A0030097biological_processhemopoiesis
A0030218biological_processerythrocyte differentiation
A0030492molecular_functionhemoglobin binding
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
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
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005833cellular_componenthemoglobin complex
C0006457biological_processprotein folding
C0020027biological_processhemoglobin metabolic process
C0030097biological_processhemopoiesis
C0030218biological_processerythrocyte differentiation
C0030492molecular_functionhemoglobin binding
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 201
ChainResidue
BPHE43
BVAL93
BASN97
BPHE98
BLEU101
BSER102
BHOH203
BHOH236
BHOH243
DMET76
DPRO77
BHIS45
DASN78
DALA79
BPHE46
BHIS58
BLYS61
BVAL62
BALA65
BLEU83
BHIS87

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM D 201
ChainResidue
BMET76
BPRO77
BASN78
BALA79
DPHE43
DHIS45
DPHE46
DHIS58
DLYS61
DVAL62
DALA65
DLEU83
DHIS87
DLEU91
DVAL93
DASN97
DPHE98
DLEU101
DSER102
DHOH204
DHOH208
DHOH227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
BGLY59
DGLY59

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
BALA88
DALA88

site_idSWS_FT_FI3
Number of Residues28
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
BASN9
BARG92
BVAL107
BLEU109
BHIS122
BTHR134
DASN9
DTRP14
DGLY25
DGLU30
DPHE46
BTRP14
DLEU48
DALA53
DLYS56
DLYS60
DARG92
DVAL107
DLEU109
DHIS122
DTHR134
BGLY25
BGLU30
BPHE46
BLEU48
BALA53
BLYS56
BLYS60

site_idSWS_FT_FI4
Number of Residues10
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
BALA12
DLEU100
BGLY57
BLYS61
BLEU91
BLEU100
DALA12
DGLY57
DLYS61
DLEU91

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BPRO4
BPHE36
BHIS50
DPRO4
DPHE36
DHIS50

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BTHR8
BVAL17
BTHR41
DTHR8
DVAL17
DTHR41

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BASN9
DASN9

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BALA12
DALA12

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BGLY25
DGLY25

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BHIS103
BLEU125
BVAL132
BLYS139
DHIS103
DLEU125
DVAL132
DLYS139

site_idSWS_FT_FI11
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
BLEU109
BVAL135
BSER138
DLEU109
DVAL135
DSER138

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
BTHR8
BVAL17
BTHR41
DTHR8
DVAL17
DTHR41

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
BVAL62
DVAL62

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PDB entries from 2024-11-06

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