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1H3J

STRUCTURE OF RECOMBINANT COPRINUS CINEREUS PEROXIDASE DETERMINED TO 2.0 A

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 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
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:8112469
ChainResidueDetails
AASN142
BASN142

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:8112469
ChainResidueDetails
ASER338
BSER338

226707

PDB entries from 2024-10-30

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