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4ESA

X-ray structure of carbonmonoxy hemoglobin of Eleginops maclovinus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion 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
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion 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
C0072562cellular_componentblood microparticle
C0098869biological_processcellular oxidant detoxification
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 201
ChainResidue
AHIS59
AVAL63
AHEM202

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 202
ChainResidue
AGLN87
AHIS88
ALEU92
AASN98
APHE99
ALEU102
ALEU137
ACMO201
AHOH356
AHOH366
AHOH369
AHOH382
ATYR42
APHE43
AHIS45
ATRP46
AHIS59
ATHR62

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 201
ChainResidue
BHIS63
BVAL67
BHEM202

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 202
ChainResidue
BTHR38
BHIS41
BPHE42
BHIS63
BLEU88
BHIS92
BLEU96
BASN102
BPHE103
BLEU106
BLEU141
BCMO201

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO C 201
ChainResidue
CHIS59
CVAL63
CHEM202

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM C 202
ChainResidue
CTYR42
CPHE43
CHIS45
CTRP46
CHIS59
CTHR62
CGLN87
CHIS88
CLEU92
CASN98
CLEU102
CLEU137
CCMO201
CHOH367

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO D 201
ChainResidue
DHIS63
DVAL67
DHEM202

site_idAC8
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM D 202
ChainResidue
DTHR38
DHIS41
DPHE42
DHIS63
DLYS66
DLEU88
DHIS92
DLYS95
DLEU96
DVAL98
DASN102
DPHE103
DLEU106
DLEU141
DCMO201
DHOH1053
DHOH1069
DHOH1112

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 203
ChainResidue
ATHR41
DARG40
DHIS41
DLYS95
DLEU96
DHIS97
DHOH1074

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: distal binding residue => ECO:0000269|PubMed:23086282
ChainResidueDetails
BHIS63
DHIS63

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:23086282
ChainResidueDetails
BHIS92
DHIS92

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000312|PDB:4ESA
ChainResidueDetails
ASER1
CSER1

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PDB entries from 2024-07-24

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