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3OVU

Crystal Structure of Human Alpha-Haemoglobin Complexed with AHSP and the First NEAT Domain of IsdH from Staphylococcus aureus

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
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005829cellular_componentcytosol
C0005833cellular_componenthemoglobin complex
C0015670biological_processcarbon dioxide transport
C0015671biological_processoxygen transport
C0016020cellular_componentmembrane
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0030185biological_processnitric oxide transport
C0031720molecular_functionhaptoglobin binding
C0031838cellular_componenthaptoglobin-hemoglobin complex
C0042542biological_processresponse to hydrogen peroxide
C0042744biological_processhydrogen peroxide catabolic process
C0043177molecular_functionorganic acid binding
C0046872molecular_functionmetal ion binding
C0070062cellular_componentextracellular exosome
C0071682cellular_componentendocytic vesicle lumen
C0072562cellular_componentblood microparticle
C0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM C 142
ChainResidue
BLYS102
CHIS89
CVAL93
CLEU101
CPHE46
CHIS58
CLYS61
CVAL62
CLEU66
CLEU83
CLEU86
CALA88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
CHIS58

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
CHIS87

site_idSWS_FT_FI3
Number of Residues14
DetailsSITE: (Microbial infection) Cleavage; by N.americanus apr-2 => ECO:0000269|PubMed:12552433
ChainResidueDetails
CTHR8
CLEU91
CLEU106
CTHR108
CVAL121
CSER133
CALA13
CTYR24
CLEU29
CHIS45
CASP47
CSER52
CVAL55
CGLY59

site_idSWS_FT_FI4
Number of Residues5
DetailsSITE: Not glycated => ECO:0000269|PubMed:7358733
ChainResidueDetails
CLYS11
CLYS56
CLYS60
CLYS90
CLYS99

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER3
CSER35
CSER49

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
CLYS7
CLYS16
CLYS40

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTHR8

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
CLYS11

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
CTYR24

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
CSER102
CSER124
CSER131
CSER138

site_idSWS_FT_FI11
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
CTHR108
CTHR134
CTHR137

site_idSWS_FT_FI12
Number of Residues3
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:7358733
ChainResidueDetails
CLYS7
CLYS16
CLYS40

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:7358733
ChainResidueDetails
CLYS61

219140

PDB entries from 2024-05-01

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