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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7LAN

CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH COMPOUND-30 AKA 7-[(3~{S},4~{R},6~{R})-4-benzyl-2-oxa-7,13,14-triazatetracyclo[14.3.1.1^{3,6}.1^{11,14}]docosa-1(19),11(21),12,16(20),17-pentaen-10-yl]-3~{H}-triazolo[4,5-b]pyridin-5-amine

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
D0004601molecular_functionperoxidase activity
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
E0004601molecular_functionperoxidase activity
E0006979biological_processresponse to oxidative stress
E0020037molecular_functionheme binding
F0004601molecular_functionperoxidase activity
F0006979biological_processresponse to oxidative stress
F0020037molecular_functionheme binding
G0004601molecular_functionperoxidase activity
G0006979biological_processresponse to oxidative stress
G0020037molecular_functionheme binding
H0004601molecular_functionperoxidase activity
H0006979biological_processresponse to oxidative stress
H0020037molecular_functionheme binding
I0004601molecular_functionperoxidase activity
I0006979biological_processresponse to oxidative stress
I0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
BGLU242-LEU252
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10766826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11705390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MHL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000220","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
BARG239electrostatic stabiliser
site_idMCSA2
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
site_idMCSA3
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
EGLY207proton shuttle (general acid/base)
site_idMCSA4
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
GGLY207proton shuttle (general acid/base)

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PDB entries from 2025-12-10

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