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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7OIH

Glycosylation in the crystal structure of neutrophil myeloperoxidase

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
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
Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
AGLU408-LEU418
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues24
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 Residues8
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues32
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 Residues8
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 Residues8
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsModified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
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 Residues16
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 Residues8
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 Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
AHIS261proton shuttle (general acid/base)
AMET409electrostatic stabiliser
site_idMCSA2
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
BHIS261proton shuttle (general acid/base)
BMET409electrostatic stabiliser
site_idMCSA3
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
CHIS261proton shuttle (general acid/base)
CMET409electrostatic stabiliser
site_idMCSA4
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
DHIS261proton shuttle (general acid/base)
DMET409electrostatic stabiliser
site_idMCSA5
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
EHIS261proton shuttle (general acid/base)
EMET409electrostatic stabiliser
site_idMCSA6
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
FHIS261proton shuttle (general acid/base)
FMET409electrostatic stabiliser
site_idMCSA7
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
GHIS261proton shuttle (general acid/base)
GMET409electrostatic stabiliser
site_idMCSA8
Number of Residues2
DetailsM-CSA 601
ChainResidueDetails
HHIS261proton shuttle (general acid/base)
HMET409electrostatic stabiliser

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PDB entries from 2025-12-10

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