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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1LFI

METAL SUBSTITUTION IN TRANSFERRINS: THE CRYSTAL STRUCTURE OF HUMAN COPPER-LACTOFERRIN AT 2.1 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0001503biological_processossification
A0001530molecular_functionlipopolysaccharide binding
A0001817biological_processregulation of cytokine production
A0002227biological_processinnate immune response in mucosa
A0002376biological_processimmune system process
A0003677molecular_functionDNA binding
A0004252molecular_functionserine-type endopeptidase activity
A0004869molecular_functioncysteine-type endopeptidase inhibitor activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005769cellular_componentearly endosome
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0006959biological_processhumoral immune response
A0008201molecular_functionheparin binding
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0009986cellular_componentcell surface
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0019732biological_processantifungal humoral response
A0030141cellular_componentsecretory granule
A0031640biological_processkilling of cells of another organism
A0031665biological_processnegative regulation of lipopolysaccharide-mediated signaling pathway
A0032680biological_processregulation of tumor necrosis factor production
A0032780biological_processnegative regulation of ATP-dependent activity
A0032991cellular_componentprotein-containing complex
A0033690biological_processpositive regulation of osteoblast proliferation
A0034145biological_processpositive regulation of toll-like receptor 4 signaling pathway
A0035580cellular_componentspecific granule lumen
A0042581cellular_componentspecific granule
A0042742biological_processdefense response to bacterium
A0043066biological_processnegative regulation of apoptotic process
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044793biological_processnegative regulation by host of viral process
A0045071biological_processnegative regulation of viral genome replication
A0045669biological_processpositive regulation of osteoblast differentiation
A0046872molecular_functionmetal ion binding
A0048525biological_processnegative regulation of viral process
A0050829biological_processdefense response to Gram-negative bacterium
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0055037cellular_componentrecycling endosome
A0060349biological_processbone morphogenesis
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
A0070062cellular_componentextracellular exosome
A0071902biological_processpositive regulation of protein serine/threonine kinase activity
A0097013cellular_componentphagocytic vesicle lumen
A0140912molecular_functionmembrane destabilizing activity
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
A1904724cellular_componenttertiary granule lumen
A2000308biological_processnegative regulation of tumor necrosis factor (ligand) superfamily member 11 production
A2001205biological_processnegative regulation of osteoclast development
Functional Information from PDB Data
site_idAN1
Number of Residues6
Details
ChainResidue
ACO3695
ATHR117
AARG121
AALA123
AGLY124
ACU693
site_idAN2
Number of Residues6
Details
ChainResidue
ACO3696
ATHR461
AARG465
AALA467
AGLY468
ACU694
site_idCU1
Number of Residues6
Details
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
ACU693
ACO3695
site_idCU2
Number of Residues6
Details
ChainResidue
AHIS597
ACU694
ACO3696
AASP395
ATYR435
ATYR528
Functional Information from PROSITE/UniProt
site_idPS00205
Number of Residues10
DetailsTRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG
ChainResidueDetails
ATYR92-GLY101
ATYR435-SER444
site_idPS00206
Number of Residues17
DetailsTRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLrdgaGDVAF
ChainResidueDetails
ATYR192-PHE208
ATYR528-PHE544
site_idPS00207
Number of Residues31
DetailsTRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLCpDntrkp...VdkfkdChlArvpsHaVV
ChainResidueDetails
AGLU226-VAL256
AASP570-VAL600
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues47
DetailsPeptide: {"description":"Lactoferricin-H","featureId":"PRO_0000422770"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues30
DetailsPeptide: {"description":"Kaliocin-1","featureId":"PRO_0000035733"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
DetailsPeptide: {"description":"Lactoferroxin-A","featureId":"PRO_0000035734"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsPeptide: {"description":"Lactoferroxin-B","featureId":"PRO_0000035735"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues6
DetailsPeptide: {"description":"Lactoferroxin-C","featureId":"PRO_0000035736"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues327
DetailsDomain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues331
DetailsDomain: {"description":"Transferrin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues9
DetailsRegion: {"description":"Bactericidal and antifungal activity"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsRegion: {"description":"Critical for glycosaminoglycan, lipid A, lysozyme and DNA binding"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsRegion: {"description":"Important for full bactericidal and antifungal activities"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues10
DetailsRegion: {"description":"Interaction with lipopolysaccharide"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsRegion: {"description":"Interaction with PspA"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues5
DetailsRegion: {"description":"Involved in glycosaminoglycan binding"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12535064","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
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_FI17
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_FI18
Number of Residues2
DetailsSite: {"description":"Interaction with PspA"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsSite: {"description":"Important for iron binding"}
ChainResidueDetails
site_idSWS_FT_FI20
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_FI21
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_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
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

239149

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