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1LFG

Structure of diferric human lactoferrin

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
A0006826biological_processiron ion transport
A0006959biological_processhumoral immune response
A0008201molecular_functionheparin binding
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0009986cellular_componentcell surface
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
A2000117biological_processnegative regulation of cysteine-type endopeptidase activity
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
DetailsCO3 BINDING SITE 1
ChainResidue
ACO3695
ATHR117
AARG121
AALA123
AGLY124
AFE693

site_idAN2
Number of Residues6
DetailsCO3 BINDING SITE 2
ChainResidue
ACO3696
ATHR461
AARG465
AALA467
AGLY468
AFE694

site_idFE1
Number of Residues6
DetailsIRON BINDING SITE 1
ChainResidue
AASP60
ATYR92
ATYR192
AHIS253
AFE693
ACO3695

site_idFE2
Number of Residues6
DetailsIRON BINDING SITE 2
ChainResidue
AHIS597
AFE694
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. YsGAFKCLkdgaGDVAF
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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064
ChainResidueDetails
ATYR72

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064
ChainResidueDetails
AARG258

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8703903, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
ChainResidueDetails
ALEU59
AHIS91
ASER191
ASER252
ALEU394
AGLY434
AGLY527
AASN596

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00741, ECO:0000269|PubMed:10089347, ECO:0000269|PubMed:10828980, ECO:0000269|PubMed:11128996, ECO:0000269|PubMed:12450380, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:17543335, ECO:0000269|PubMed:22900286, ECO:0000269|PubMed:8371268, ECO:0000269|PubMed:8594202, ECO:0000269|PubMed:8931543, ECO:0000269|PubMed:9003186, ECO:0000269|Ref.72
ChainResidueDetails
AHIS116
AARG120
ATHR122
AALA123
AHIS460
AASP464
ATHR466
AALA467

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interaction with PspA
ChainResidueDetails
AARG3
ASER12

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for iron binding
ChainResidueDetails
AILE209

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299444, ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8069634, ECO:0000269|Ref.72
ChainResidueDetails
ALEU136

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15299793, ECO:0000269|PubMed:1581307, ECO:0000269|PubMed:16201406, ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.72
ChainResidueDetails
APHE477

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
ChainResidueDetails
AARG622

226707

PDB entries from 2024-10-30

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