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3ZS0

Human Myeloperoxidase inactivated by TX2

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
C0004601molecular_functionperoxidase activity
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
D0004601molecular_functionperoxidase activity
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
CGLU242-LEU252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
CMET190
DMET190

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
CASN189
CTHR337
CLEU338
DASN189
DTHR337
DLEU338

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
CSER191
DSER191

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
ChainResidueDetails
CGLU263
CLYS265
CLEU267
CPRO269
DGLU263
DLYS265
DLEU267
DPRO269

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
CPRO431
DPRO431

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
CTYR334
DTYR334

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
ChainResidueDetails
CGLU245
DGLU245

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
ChainResidueDetails
CLEU252
DLEU252

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
CVAL284
CVAL320
DVAL284
DVAL320

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
CARG412
DARG412

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
CMET190proton shuttle (general acid/base)
CTYR334electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
DMET190proton shuttle (general acid/base)
DTYR334electrostatic stabiliser

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PDB entries from 2024-10-30

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