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1D7W

CRYSTAL STRUCTURE OF HUMAN MYELOPEROXIDASE ISOFORM C COMPLEXED WITH CYANIDE AND BROMIDE AT PH 4.0

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 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
CTHR168
CPHE170
CASP172
CSER174
DTHR168
DPHE170
DASP172
DSER174

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
CGLU242
CMET243
DGLU242
DMET243

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
CHIS336
DHIS336

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
CARG239
DARG239

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
ChainResidueDetails
CCSO150
DCSO150

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
ChainResidueDetails
CASN157
DASN157

site_idSWS_FT_FI7
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
CASN189
CASN225
DASN189
DASN225

site_idSWS_FT_FI8
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
CASN317
DASN317

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087
ChainResidueDetails
CASN563
DASN563

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
CARG239electrostatic stabiliser

site_idMCSA2
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
DARG239electrostatic stabiliser

220113

PDB entries from 2024-05-22

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