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1LYC

The impact of the physical and chemical enviroment on the molecular structure of Coprinus cinereus peroxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
B0000302biological_processresponse to reactive oxygen species
B0004601molecular_functionperoxidase activity
B0005576cellular_componentextracellular region
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
B0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 9001
ChainResidue
ASER184
AASP201
ATHR203
AVAL206
AASP208

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 9002
ChainResidue
BASP208
BSER184
BASP201
BTHR203
BVAL206

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 9003
ChainResidue
AASP56
AGLY74
AASP76
ASER78
AHOH9009
AHOH9044

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 9004
ChainResidue
BASP56
BGLY74
BASP76
BSER78
BHOH9016

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 344
ChainResidue
AARG47
ALEU50
AARG51
APHE54
APRO153
AGLY154
APRO155
ALEU179
ALEU180
AALA182
AHIS183
ALEU185
AALA186
ASER187
AGLN188
AGLU189
AGLY190
ALEU191
AMET242
ASER244
AMET276
AHOH9041
AHOH9078
AHOH9120

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 344
ChainResidue
BARG47
BLEU50
BARG51
BPHE54
BPRO153
BGLY154
BPRO155
BLEU179
BLEU180
BALA182
BHIS183
BLEU185
BALA186
BSER187
BGLN188
BGLU189
BGLY190
BLEU191
BMET242
BSER244
BMET276
BHOH9007
BHOH9011
BHOH9076

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVDLLAAHSL
ChainResidueDetails
AGLU175-LEU185

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. VRkiLRIvFHDA
ChainResidueDetails
AVAL46-ALA57

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"8112469","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"8112469","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

数据于2025-07-23公开中

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