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3BOM

Crystal structure of trout hemoglobin at 1.35 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005344molecular_functionoxygen carrier activity
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
B0004601molecular_functionperoxidase activity
B0005344molecular_functionoxygen carrier activity
B0005833cellular_componenthemoglobin complex
B0015671biological_processoxygen transport
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0031720molecular_functionhaptoglobin binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0072562cellular_componentblood microparticle
B0098869biological_processcellular oxidant detoxification
C0004601molecular_functionperoxidase activity
C0005344molecular_functionoxygen carrier activity
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
D0004601molecular_functionperoxidase activity
D0005344molecular_functionoxygen carrier activity
D0005833cellular_componenthemoglobin complex
D0015671biological_processoxygen transport
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0031720molecular_functionhaptoglobin binding
D0031838cellular_componenthaptoglobin-hemoglobin complex
D0042744biological_processhydrogen peroxide catabolic process
D0043177molecular_functionorganic acid binding
D0046872molecular_functionmetal ion binding
D0072562cellular_componentblood microparticle
D0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 143
ChainResidue
ATYR42
AVAL94
AASN98
APHE99
ALEU102
ALEU137
AHOH225
AHOH246
AHOH251
AHOH263
AHOH318
APHE43
AHOH319
AHOH321
AHOH343
AHOH345
AHIS45
ATRP46
AHIS59
ATHR62
ALEU87
AHIS88
ALEU92

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 148
ChainResidue
BHIS41
BPHE45
BHIS63
BVAL67
BMET91
BHIS92
BLEU96
BASN102
BPHE103
BLEU106
BLEU142
BHOH2941
BHOH2958
DLYS95

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM C 143
ChainResidue
CTYR42
CPHE43
CHIS45
CTRP46
CHIS59
CTHR62
CHIS88
CLEU92
CVAL94
CASN98
CLEU102
CLEU137
CEDO2775
CHOH2837
CHOH2889
CHOH2925
CHOH2942
CHOH2949
CHOH2951
CHOH2959
CHOH2980

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM D 148
ChainResidue
DHIS63
DVAL67
DLEU88
DMET91
DHIS92
DLEU96
DASN102
DPHE103
DLEU106
DLEU142
DHOH2903
DHOH2934
DHOH2957

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 2775
ChainResidue
AHOH166
BARG104
BALA107
BASP108
BGLN132
BHOH2836
BHOH2978

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO D 2775
ChainResidue
DARG104
DALA107
DASP108
DGLN132
DVAL139
DHOH2811
DHOH2918

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 2775
ChainResidue
CTRP46
CLYS58
CHIS59
CTHR62
CHEM143
CHOH2830
CHOH2964

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO C 2776
ChainResidue
CGLU26
CSER30
CPRO51
CGLY52
CHOH2781
CHOH2953

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"2706274","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues290
DetailsDomain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"distal binding residue"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue"}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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