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3HYU

Crystal structure of the altitude adapted hemoglobin of guinea pig.

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
B0031721molecular_functionhemoglobin alpha 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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM A 142
ChainResidue
ATYR42
APHE98
ALEU101
ALEU136
AHOH172
AHOH214
APHE43
AHIS45
AHIS58
ALYS61
ALEU83
AHIS87
ALEU91
AASN97

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 143
ChainResidue
APHE36
APHE100
BASN108

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE HEM B 147
ChainResidue
BPHE41
BPHE42
BLYS44
BHIS63
BVAL67
BHIS92
BLEU96
BASN102
BLEU106
BLEU141
BHOH165
BHOH199

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 148
ChainResidue
BTHR123
BHOH155
BHOH191
BHOH214

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 149
ChainResidue
BVAL1
BLEU78
BLEU81
BLYS82
BHOH176

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 150
ChainResidue
BHIS117
BHIS118
BPRO119
BSER120
BGLU121
BHOH222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: distal binding residue
ChainResidueDetails
BHIS63

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: proximal binding residue
ChainResidueDetails
BHIS92

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylvaline => ECO:0000250|UniProtKB:P02086
ChainResidueDetails
BVAL1
ASER35
ASER49

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BLYS82
BLYS144
ALYS40

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871
ChainResidueDetails
BCYS93

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905
ChainResidueDetails
ATYR24

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ATHR108
ATHR134
ATHR137

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942
ChainResidueDetails
ASER124
ASER131
ASER138

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PDB entries from 2024-06-12

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