Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3A0G

Crystal structure analysis of guinea pig oxyhemoglobin at 2.5 angstroms 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
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 Residues11
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ATYR42
ALEU101
AOXY301
APHE43
AHIS45
AHIS58
ALYS61
AHIS87
ALEU91
AASN97
APHE98

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY A 301
ChainResidue
AHIS58
AVAL62
AHEM201

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE HEM B 401
ChainResidue
BPHE41
BPHE42
BLYS44
BHIS63
BHIS92
BLEU96
BASN102
BLEU141
BOXY501

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OXY B 501
ChainResidue
BHIS63
BVAL67
BHEM401

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon