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8OGI

Structure of native human eosinophil peroxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETPKLAAMHTL
ChainResidueDetails
BGLU380-LEU390

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
BTHR306
BPHE308
BASP310
BSER312

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: covalent
ChainResidueDetails
BGLU380

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
BHIS474

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00298
ChainResidueDetails
BARG377

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:18694936
ChainResidueDetails
BTYR488

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN327
BASN363
BASN700
BASN708

227561

PDB entries from 2024-11-20

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