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1BGP

CRYSTAL STRUCTURE OF BARLEY GRAIN PEROXIDASE 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 501
ChainResidue
ATHR180
AASP225
ATHR228
AVAL231
AASP233

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 502
ChainResidue
ASER59
AASP50
AVAL53
AGLY55
AASP57

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 400
ChainResidue
AALA41
AARG45
APHE48
AARG81
APRO149
AGLY150
APRO151
AILE175
AGLY178
AHIS179
AGLY182
ALEU183
AALA184
AHIS185
ASER188
AARG221
ALEU224
APHE247
ASER249
AHOH620
AHOH706
AHOH707
AHOH757

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVTISGGHTI
ChainResidueDetails
AASP171-ILE181

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AAglLRLhFHDC
ChainResidueDetails
AALA40-CYS51

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 7atj
ChainResidueDetails
AHIS49
AARG45
AASN77

221716

PDB entries from 2024-06-26

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