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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1BLF

STRUCTURE OF DIFERRIC BOVINE LACTOFERRIN AT 2.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0001503biological_processossification
A0001817biological_processregulation of cytokine production
A0002227biological_processinnate immune response in mucosa
A0002376biological_processimmune system process
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0019732biological_processantifungal humoral response
A0031665biological_processnegative regulation of lipopolysaccharide-mediated signaling pathway
A0032680biological_processregulation of tumor necrosis factor production
A0033690biological_processpositive regulation of osteoblast proliferation
A0042581cellular_componentspecific granule
A0042742biological_processdefense response to bacterium
A0043066biological_processnegative regulation of apoptotic process
A0045669biological_processpositive regulation of osteoblast differentiation
A0046872molecular_functionmetal ion binding
A0051241biological_processnegative regulation of multicellular organismal process
A0055037cellular_componentrecycling endosome
A0060349biological_processbone morphogenesis
A1900159biological_processpositive regulation of bone mineralization involved in bone maturation
A1900229biological_processnegative regulation of single-species biofilm formation in or on host organism
A1902732biological_processpositive regulation of chondrocyte proliferation
A2000308biological_processnegative regulation of tumor necrosis factor (ligand) superfamily member 11 production
A2001205biological_processnegative regulation of osteoclast development
Functional Information from PDB Data
site_idFE1
Number of Residues5
DetailsFE+3 BINDING SITE.
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACO3702
site_idFE2
Number of Residues5
DetailsFE+3 BINDING SITE.
ChainResidue
ACO3703
AASP395
ATYR433
ATYR526
AHIS595
Functional Information from PROSITE/UniProt
site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLqdgaGDVAF
ChainResidueDetails
ATYR192-PHE208
ATYR526-PHE542
site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClNnsrap...VdafkeChlAqvpsHaVV
ChainResidueDetails
AGLN226-VAL256
AASP568-VAL598
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101
ATYR433-ALA442
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsPeptide: {"description":"Lactoferricin-B","featureId":"PRO_0000035727"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues327
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues329
DetailsDomain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9398529","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BLF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2021","firstPage":"104999","lastPage":"104999","volume":"119","journal":"Int. Dairy J.","title":"Comprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MSComprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MS.","authors":["Gnanesh Kumar B.S.","Mattad S."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.idairyj.2021.104999"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2021","firstPage":"104999","lastPage":"104999","volume":"119","journal":"Int. Dairy J.","title":"Comprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MSComprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MS.","authors":["Gnanesh Kumar B.S.","Mattad S."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.idairyj.2021.104999"}]}}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; alternate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9398529","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2021","firstPage":"104999","lastPage":"104999","volume":"119","journal":"Int. Dairy J.","title":"Comprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MSComprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MS.","authors":["Gnanesh Kumar B.S.","Mattad S."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.idairyj.2021.104999"}]}},{"source":"PDB","id":"1BLF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9398529","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2021","firstPage":"104999","lastPage":"104999","volume":"119","journal":"Int. Dairy J.","title":"Comprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MSComprehensive analysis of lactoferrin N-glycans with site-specificity from bovine colostrum using specific proteases and RP-UHPLC-MS/MS.","authors":["Gnanesh Kumar B.S.","Mattad S."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.idairyj.2021.104999"}]}},{"source":"PDB","id":"1BLF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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