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1A8U

CHLOROPEROXIDASE T/BENZOATE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004601molecular_functionperoxidase activity
A0016491molecular_functionoxidoreductase activity
A0016691molecular_functionchloride peroxidase activity
A0098869biological_processcellular oxidant detoxification
B0003824molecular_functioncatalytic activity
B0004601molecular_functionperoxidase activity
B0016491molecular_functionoxidoreductase activity
B0016691molecular_functionchloride peroxidase activity
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 290
ChainResidue
AHOH305
AHOH448
AHOH559
AHOH562
AHOH590
ASER35
AHIS37
ATHR189

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 292
ChainResidue
AARG106
ATHR207
AHOH313
AHOH477
AHOH484
AHOH500
AHOH602
AHOH629

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 294
ChainResidue
ALEU244
APRO245
ASER246
AHOH613

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 291
ChainResidue
BSER35
BHIS37
BTHR189
BHOH307
BHOH309
BHOH419
BHOH465
BHOH486
BHOH628
BHOH629

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 293
ChainResidue
BARG106
BHOH317
BHOH445
BHOH461
BHOH477
BHOH481
BHOH517

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEZ A 295
ChainResidue
AGLY31
APHE32
APHE97
ASER98
AMET99
ATRP205
ATHR230
AHIS257
AHOH411

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BEZ B 294
ChainResidue
BGLY31
BPHE32
BPHE97
BSER98
BMET99
BTRP205
BTHR230
BHIS257
BHOH492

site_idNUA
Number of Residues3
DetailsCATALYTIC TRIAD.
ChainResidue
ASER98
AASP228
AHIS257

site_idNUB
Number of Residues3
DetailsCATALYTIC TRIAD.
ChainResidue
BSER98
BASP228
BHIS257

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P22862
ChainResidueDetails
ASER98
AASP228
AHIS257
BSER98
BASP228
BHIS257

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a7u
ChainResidueDetails
ASER98
AASP228
AHIS257
APHE32
AMET99

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a7u
ChainResidueDetails
BSER98
BASP228
BHIS257
BPHE32
BMET99

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a7u
ChainResidueDetails
ASER98
AHIS257
AASP228

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a7u
ChainResidueDetails
BSER98
BHIS257
BASP228

site_idMCSA1
Number of Residues5
DetailsM-CSA 248
ChainResidueDetails
APHE32electrostatic stabiliser, hydrogen bond donor
ASER98covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AMET99electrostatic stabiliser, hydrogen bond donor
AASP228hydrogen bond acceptor, increase acidity, increase basicity
AHIS257hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 248
ChainResidueDetails
BPHE32electrostatic stabiliser, hydrogen bond donor
BSER98covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BMET99electrostatic stabiliser, hydrogen bond donor
BASP228hydrogen bond acceptor, increase acidity, increase basicity
BHIS257hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-06-18

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