Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3FAQ

Crystal structure of lactoperoxidase complex with cyanide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P05164","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P05164","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P11678","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine; alternate","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30296068","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30296068","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; alternate","evidences":[{"source":"PubMed","id":"19339248","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30296068","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Buffalo lactoperoxidase at 2.75A resolution.","authors":["Sheikh I.A.","Ethayathulla A.S.","Singh A.K.","Singh N.","Sharma S.","Singh T.P."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2007","submissionDatabase":"PDB data bank","title":"Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution.","authors":["Sheikh I.A.","Jain R.","Singh N.","Sharma S.","Bhushan A.","Kaur P.","Srinivasan A.","Singh T.P."]}}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mhl
ChainResidueDetails
AHIS109
AGLN105
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mhl
ChainResidueDetails
AARG255
site_idMCSA1
Number of Residues9
DetailsM-CSA 944
ChainResidueDetails
AGLN105transition state stabiliser
AASP108alter redox potential, covalently attached
AASP110metal ligand
ATHR184metal ligand
APHE186metal ligand
AASP188metal ligand
ASER190metal ligand
ALEU262alter redox potential, covalently attached
APRO355metal ligand

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon