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1F5P

2.9 ANGSTROM CRYSTAL STRUCTURE OF LAMPREY HEMOGLOBIN THAT HAS BEEN EXPOSED TO CARBON MONOXIDE.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005344molecular_functionoxygen carrier activity
A0005506molecular_functioniron ion binding
A0015671biological_processoxygen transport
A0016491molecular_functionoxidoreductase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0005344molecular_functionoxygen carrier activity
B0005506molecular_functioniron ion binding
B0015671biological_processoxygen transport
B0016491molecular_functionoxidoreductase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0005344molecular_functionoxygen carrier activity
C0005506molecular_functioniron ion binding
C0015671biological_processoxygen transport
C0016491molecular_functionoxidoreductase activity
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0005344molecular_functionoxygen carrier activity
D0005506molecular_functioniron ion binding
D0015671biological_processoxygen transport
D0016491molecular_functionoxidoreductase activity
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
E0005344molecular_functionoxygen carrier activity
E0005506molecular_functioniron ion binding
E0015671biological_processoxygen transport
E0016491molecular_functionoxidoreductase activity
E0019825molecular_functionoxygen binding
E0020037molecular_functionheme binding
E0046872molecular_functionmetal ion binding
F0005344molecular_functionoxygen carrier activity
F0005506molecular_functioniron ion binding
F0015671biological_processoxygen transport
F0016491molecular_functionoxidoreductase activity
F0019825molecular_functionoxygen binding
F0020037molecular_functionheme binding
F0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 150
ChainResidue
APHE51
AVAL111
ATYR115
APHE116
ALEU119
ALEU145
ACMO151
APHE52
ALYS54
AHIS73
AARG76
AALA80
ALYS104
AHIS105
APHE109

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 151
ChainResidue
AHIS73
AILE77
AHEM150

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 150
ChainResidue
BPHE51
BLYS54
BHIS73
BARG76
BLYS104
BHIS105
BPHE109
BVAL111
BTYR115
BPHE116
BLEU119
BLEU145
BCMO151

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 151
ChainResidue
BHIS73
BILE77
BHEM150

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM C 150
ChainResidue
CPHE51
CPHE52
CLYS54
CHIS73
CARG76
CILE77
CLEU101
CLYS104
CHIS105
CPHE109
CVAL111
CTYR115
CPHE116
CLEU145
CCMO151

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO C 151
ChainResidue
CHIS73
CILE77
CHEM150

site_idAC7
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM D 150
ChainResidue
DPHE51
DPHE52
DLYS54
DHIS73
DARG76
DALA80
DLYS104
DHIS105
DPHE109
DTYR115
DPHE116
DLEU119
DLEU145
DCMO151

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO D 151
ChainResidue
DHIS73
DILE77
DHEM150

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM E 150
ChainResidue
EPHE51
EPHE52
ELYS54
EHIS73
EARG76
ELYS104
EHIS105
EPHE109
EVAL111
ETYR115
EPHE116
ELEU119
ELEU145
ECMO151

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO E 151
ChainResidue
EHIS73
EILE77
EHEM150

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM F 150
ChainResidue
FCMO151
FPHE51
FPHE52
FLYS54
FHIS73
FARG76
FILE77
FLYS104
FHIS105
FPHE109
FVAL111
FTYR115
FPHE116
FLEU145

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO F 151
ChainResidue
FHIS73
FILE77
FHEM150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:4032476
ChainResidueDetails
AHIS73
BHIS73
CHIS73
DHIS73
EHIS73
FHIS73

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:4032476
ChainResidueDetails
AHIS105
BHIS105
CHIS105
DHIS105
EHIS105
FHIS105

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PDB entries from 2024-07-17

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