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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2BJJ

Structure of recombinant human lactoferrin produced in the milk of transgenic cows

Functional Information from GO Data
ChainGOidnamespacecontents
X0001503biological_processossification
X0001530molecular_functionlipopolysaccharide binding
X0001817biological_processregulation of cytokine production
X0002227biological_processinnate immune response in mucosa
X0002376biological_processimmune system process
X0003677molecular_functionDNA binding
X0004252molecular_functionserine-type endopeptidase activity
X0004869molecular_functioncysteine-type endopeptidase inhibitor activity
X0005506molecular_functioniron ion binding
X0005515molecular_functionprotein binding
X0005576cellular_componentextracellular region
X0005615cellular_componentextracellular space
X0005634cellular_componentnucleus
X0005737cellular_componentcytoplasm
X0005769cellular_componentearly endosome
X0005886cellular_componentplasma membrane
X0006351biological_processDNA-templated transcription
X0006508biological_processproteolysis
X0006811biological_processmonoatomic ion transport
X0006826biological_processiron ion transport
X0006959biological_processhumoral immune response
X0008201molecular_functionheparin binding
X0008233molecular_functionpeptidase activity
X0008236molecular_functionserine-type peptidase activity
X0009986cellular_componentcell surface
X0016787molecular_functionhydrolase activity
X0019731biological_processantibacterial humoral response
X0019732biological_processantifungal humoral response
X0030141cellular_componentsecretory granule
X0031640biological_processkilling of cells of another organism
X0031665biological_processnegative regulation of lipopolysaccharide-mediated signaling pathway
X0032680biological_processregulation of tumor necrosis factor production
X0032991cellular_componentprotein-containing complex
X0033690biological_processpositive regulation of osteoblast proliferation
X0034145biological_processpositive regulation of toll-like receptor 4 signaling pathway
X0035580cellular_componentspecific granule lumen
X0042581cellular_componentspecific granule
X0042742biological_processdefense response to bacterium
X0043066biological_processnegative regulation of apoptotic process
X0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
X0043539molecular_functionprotein serine/threonine kinase activator activity
X0044793biological_processhost-mediated suppression of viral proces
X0044828biological_processhost-mediated suppression of viral genome replication
X0045669biological_processpositive regulation of osteoblast differentiation
X0046872molecular_functionmetal ion binding
X0050829biological_processdefense response to Gram-negative bacterium
X0055037cellular_componentrecycling endosome
X0060349biological_processbone morphogenesis
X0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
X0070062cellular_componentextracellular exosome
X0097013cellular_componentphagocytic vesicle lumen
X0140912molecular_functionmembrane destabilizing activity
X1900159biological_processpositive regulation of bone mineralization involved in bone maturation
X1900229biological_processnegative regulation of single-species biofilm formation in or on host organism
X1902732biological_processpositive regulation of chondrocyte proliferation
X1904724cellular_componenttertiary granule lumen
X2000308biological_processnegative regulation of tumor necrosis factor (ligand) superfamily member 11 production
X2001205biological_processnegative regulation of osteoclast development
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
XTYR93-GLY102
XTYR436-SER445
site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
ChainResidueDetails
XTYR193-PHE209
XTYR529-PHE545
site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
ChainResidueDetails
XGLU227-VAL257
XASP571-VAL601
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsPeptide: {"description":"Kaliocin-1","featureId":"PRO_0000035733"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues5
DetailsPeptide: {"description":"Lactoferroxin-A","featureId":"PRO_0000035734"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsPeptide: {"description":"Lactoferroxin-B","featureId":"PRO_0000035735"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsPeptide: {"description":"Lactoferroxin-C","featureId":"PRO_0000035736"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues327
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues331
DetailsDomain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsRegion: {"description":"Important for full bactericidal and antifungal activities"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues10
DetailsRegion: {"description":"Interaction with lipopolysaccharide"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsRegion: {"description":"Interaction with PspA"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsRegion: {"description":"Involved in glycosaminoglycan binding"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10089347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10828980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12450380","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17543335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22900286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8703903","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931543","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9003186","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10089347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10828980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11128996","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12450380","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1581307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17543335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22900286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8594202","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8931543","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9003186","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Interaction with PspA"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsSite: {"description":"Important for iron binding"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15299444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1581307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8069634","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15299793","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1581307","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16201406","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2004","submissionDatabase":"PDB data bank","title":"Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.","authors":["Vikram P.","Prem Kumar R.","Singh N.","Kumar J.","Ethayathulla A.S.","Sharma S.","Kaur P.","Singh T.P."]}}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"20404350","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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