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4BM3

CRYSTAL STRUCTURE OF MANGANESE PEROXIDASE 4 FROM PLEUROTUS OSTREATUS - CRYSTAL FORM III

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP49
AGLY67
AASP69
ASER71
AHOH2077
AHOH2083

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AASP199
AASP201
ASER177
AASP194
ATHR196

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AGLU37
AHIS40
AGLU41
AARG44
APHE47
AGLU147
APRO148
ALEU173
ASER175
AHIS176
AALA179
AALA180
AGLN181
AASP182
ATHR183
AILE184
APHE193
ASER237
AMET269
AHOH2062
AHOH2072
AHOH2078

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1339
ChainResidue
AASN12
AILE283
AASP284
AHOH2329
AHOH2331

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1340
ChainResidue
AARG295
ALYS297
AGLN298
AHOH2340
AHOH2395

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1341
ChainResidue
AGLY294
AARG295

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALLASHSV
ChainResidueDetails
AGLU168-VAL178

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. VHesLRLtFHDA
ChainResidueDetails
AVAL39-ALA50

223532

PDB entries from 2024-08-07

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