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1LY9

The impact of the physical and chemical environment 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
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
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 B 9001
ChainResidue
BSER184
BASP201
BTHR203
BVAL206
BASP208

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 9002
ChainResidue
AASP208
ASER184
AASP201
ATHR203
AVAL206

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 9003
ChainResidue
AASP56
AGLY74
AASP76
ASER78
AHOH1009
AHOH1027

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 9004
ChainResidue
BASP56
BGLY74
BASP76
BSER78
BHOH2009
BHOH2027

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 344
ChainResidue
AARG47
ALEU50
AARG51
APHE54
AGLY154
APRO155
ALEU180
AALA182
AHIS183
ALEU185
AALA186
ASER187
AGLU189
AGLY190
ALEU191
AMET242
ASER244
AMET276
AHOH1010
AHOH1011
AHOH1014
AHOH3054

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 344
ChainResidue
AHOH3091
BARG47
BLEU50
BARG51
BPHE54
BGLY154
BPRO155
BLEU179
BLEU180
BALA182
BHIS183
BLEU185
BALA186
BSER187
BGLU189
BGLY190
BLEU191
BMET242
BSER244
BMET276
BHOH2010
BHOH2011
BHOH2014

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS55
BHIS55

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASP56
BASP56
BGLY74
BASP76
BSER78
BSER184
BASP201
BTHR203
BVAL206
BASP208
AGLY74
AASP76
ASER78
ASER184
AASP201
ATHR203
AVAL206
AASP208

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS183
BHIS183

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG51
BARG51

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8477731
ChainResidueDetails
AGLN1
BGLN1

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:8112469
ChainResidueDetails
ASER142
BSER142

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:8112469
ChainResidueDetails
AALA338
BALA338

220113

PDB entries from 2024-05-22

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