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3PEL

Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity

Replaces:  3N48
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 Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
ALEU91
AVAL93
AASN97
APHE98
ALEU101
ALEU136
AHOH147
AHOH253
AHOH274
AHOH421
APHE43
AHOH451
AHIS45
APHE46
AHIS58
ALYS61
ALEU83
ALEU86
AHIS87

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BTHR38
BPHE41
BPHE42
BHIS63
BSER70
BPHE71
BLEU88
BHIS92
BLEU96
BASN102
BPHE103
BLEU106
BLEU141
BHOH213
BHOH336
BHOH375
BHOH416
BHOH452

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS58

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238
ChainResidueDetails
AHIS87

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ASER3
ASER35
ASER49

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALYS7
ALYS11
ALYS40

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ATHR8
BLYS82
BLYS144

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ALYS16

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ATYR24

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ASER102
ASER124
ASER138

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR108
ATHR134
ATHR137

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PDB entries from 2024-10-16

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