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1G0B

CARBONMONOXY LIGANDED EQUINE HEMOGLOBIN PH 8.5

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
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
B0031721molecular_functionhemoglobin alpha binding
B0031838cellular_componenthaptoglobin-hemoglobin complex
B0042744biological_processhydrogen peroxide catabolic process
B0043177molecular_functionorganic acid binding
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
AVAL93
AASN97
APHE98
ALEU101
ALEU136
ACMO143
APHE43
AHIS45
APHE46
AHIS58
ALYS61
ALEU86
AHIS87
ALEU91

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO A 143
ChainResidue
AHIS58
AVAL62
AHEM142

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BPHE41
BPHE42
BHIS63
BLYS66
BSER70
BPHE71
BLEU91
BHIS92
BLEU96
BASN102
BLEU106
BLEU141
BCMO148

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CMO B 148
ChainResidue
BHIS63
BVAL67
BHEM147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue => ECO:0000250|UniProtKB:P80044
ChainResidueDetails
BHIS63

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000269|PubMed:561852, ECO:0007744|PDB:1G0B, ECO:0007744|PDB:1IBE, ECO:0007744|PDB:1IWH, ECO:0007744|PDB:1NS6, ECO:0007744|PDB:1NS9, ECO:0007744|PDB:1Y8H, ECO:0007744|PDB:1Y8I, ECO:0007744|PDB:1Y8K, ECO:0007744|PDB:2D5X, ECO:0007744|PDB:2DHB, ECO:0007744|PDB:2MHB, ECO:0007744|PDB:2ZLT, ECO:0007744|PDB:2ZLU, ECO:0007744|PDB:2ZLV, ECO:0007744|PDB:2ZLW, ECO:0007744|PDB:2ZLX
ChainResidueDetails
BHIS92

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086
ChainResidueDetails
BVAL1
AHIS50

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BSER44
AALA12
ATHR41

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BLYS59
BLYS82
BLYS144

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BCYS93

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
AGLY25

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
AHIS103
ALEU125
AVAL132
ALYS139

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALEU109
AVAL135
ASER138

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PDB entries from 2024-11-06

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