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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
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
X0032780biological_processnegative regulation of ATP-dependent activity
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_processnegative regulation by host of viral process
X0045071biological_processnegative regulation of viral genome replication
X0045669biological_processpositive regulation of osteoblast differentiation
X0046872molecular_functionmetal ion binding
X0048525biological_processnegative regulation of viral process
X0050829biological_processdefense response to Gram-negative bacterium
X0051092biological_processpositive regulation of NF-kappaB transcription factor activity
X0055037cellular_componentrecycling endosome
X0060349biological_processbone morphogenesis
X0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
X0070062cellular_componentextracellular exosome
X0071902biological_processpositive regulation of protein serine/threonine kinase activity
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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:12535064
ChainResidueDetails
XLYS74

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12535064
ChainResidueDetails
XSER260

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
XASP61
XTYR93
XTYR193
XHIS254
XASP396
XTYR436
XTYR529
XHIS598

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
XTHR118
XARG122
XALA124
XGLY125
XTHR462
XARG466
XALA468
XGLY469

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interaction with PspA
ChainResidueDetails
XARG5
XGLN14

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for iron binding
ChainResidueDetails
XARG211

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
XASN138

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
XASN479

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18780401
ChainResidueDetails
XASN624

237992

PDB entries from 2025-06-25

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