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1H5K

X-ray induced reduction of horseradish peroxidase C1A Compound III (78-89% dose)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005773cellular_componentvacuole
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
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 Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 400
ChainResidue
ALYS65
APHE77
AARG302

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP43
AVAL46
AGLY48
AASP50
ASER52
AHOH2099

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
ATHR171
AASP222
ATHR225
AILE228
AASP230

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AARG31
AALA34
ASER35
AARG38
APHE41
ASER73
APRO139
AALA140
APRO141
APHE152
ALEU166
ASER167
AGLY169
AHIS170
APHE172
AGLY173
ALYS174
AASN175
AGLN176
APHE179
APHE221
ASER246
AHOH2053
AHOH2372
AHOH2373

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEO A 501
ChainResidue
AARG206
AHOH2239

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEO A 502
ChainResidue
AASN47
AASP50
AASN57
ATHR288
ALEU290
APEO503
AHOH2070

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEO A 503
ChainResidue
AASN57
AARG62
ATHR63
AASP66
ALEU290
APEO502

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVALSGGHTF
ChainResidueDetails
AASP162-PHE172

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AAsiLRLhFHDC
ChainResidueDetails
AALA33-CYS44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS42

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING:
ChainResidueDetails
AASP43
ATHR225
AASP230
AVAL46
AGLY48
AASP50
ASER52
AGLU64
APRO139
ATHR171
AASP222

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS170

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG38

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:1001465
ChainResidueDetails
AGLN1

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1001465
ChainResidueDetails
AASN13
AASN57

site_idSWS_FT_FI7
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN158
AASN186
AASN198
AASN214
AASN255
AASN268

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 239
ChainResidueDetails
AARG38electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS42electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASN70electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
AHIS170metal ligand

218853

PDB entries from 2024-04-24

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