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2YLJ

Horse Radish Peroxidase, mutant S167Y

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005773cellular_componentvacuole
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 Residues28
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AARG31
APRO141
ALEU148
APHE152
ALEU166
ATYR167
AGLY169
AHIS170
AGLY173
ALYS174
AASN175
AALA34
AGLN176
APHE179
APHE221
AILE244
ASER246
AACT1309
AHOH2084
AHOH2090
AHOH2091
ASER35
AARG38
APHE41
ASER73
AARG75
APRO139
AALA140

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1307
ChainResidue
AASP43
AVAL46
AGLY48
AASP50
ASER52
AHOH2101

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1308
ChainResidue
ATHR171
AASP222
ATHR225
AILE228
AASP230

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT A 1309
ChainResidue
AARG38
APHE41
AHIS42
ALEU138
APRO139
AHEM350
AHOH2090
AHOH2257
AHOH2431

Functional Information from PROSITE/UniProt
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

226707

PDB entries from 2024-10-30

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