Structure of PDB 1b0l Chain A

Receptor sequence
>1b0lA (length=691) Species: 9606 (Homo sapiens) [Search protein sequence]
GRRRSVQWCTVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIA
ENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKK
GGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVA
RFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLR
DGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARV
PSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLF
KDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAV
GEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVY
TAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTW
NSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPR
SNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTV
LQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVV
SRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECL
ARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
3D structure
PDB1b0l Structure of recombinant human lactoferrin expressed in Aspergillus awamori.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE A D60 Y92 Y192 H253 D60 Y92 Y192 H253
BS02 FE A D395 Y435 Y528 H597 D395 Y435 Y528 H597
BS03 CO3 A D60 T117 R121 T122 A123 Y192 H253 D60 T117 R121 T122 A123 Y192 H253
BS04 CO3 A D395 T461 R465 A467 Y528 D395 T461 R465 A467 Y528
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0003677 DNA binding
GO:0004252 serine-type endopeptidase activity
GO:0004869 cysteine-type endopeptidase inhibitor activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008201 heparin binding
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0043539 protein serine/threonine kinase activator activity
GO:0046872 metal ion binding
GO:0140912 membrane destabilizing activity
Biological Process
GO:0001503 ossification
GO:0001817 regulation of cytokine production
GO:0002227 innate immune response in mucosa
GO:0002376 immune system process
GO:0006508 proteolysis
GO:0006826 iron ion transport
GO:0006959 humoral immune response
GO:0019731 antibacterial humoral response
GO:0019732 antifungal humoral response
GO:0031640 killing of cells of another organism
GO:0031665 negative regulation of lipopolysaccharide-mediated signaling pathway
GO:0032680 regulation of tumor necrosis factor production
GO:0032780 negative regulation of ATP-dependent activity
GO:0033690 positive regulation of osteoblast proliferation
GO:0034145 positive regulation of toll-like receptor 4 signaling pathway
GO:0042742 defense response to bacterium
GO:0043066 negative regulation of apoptotic process
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0044793 negative regulation by host of viral process
GO:0045071 negative regulation of viral genome replication
GO:0045669 positive regulation of osteoblast differentiation
GO:0048525 negative regulation of viral process
GO:0050829 defense response to Gram-negative bacterium
GO:0051092 positive regulation of NF-kappaB transcription factor activity
GO:0060349 bone morphogenesis
GO:0061844 antimicrobial humoral immune response mediated by antimicrobial peptide
GO:0071902 positive regulation of protein serine/threonine kinase activity
GO:1900159 positive regulation of bone mineralization involved in bone maturation
GO:1900229 negative regulation of single-species biofilm formation in or on host organism
GO:1902732 positive regulation of chondrocyte proliferation
GO:2000117 negative regulation of cysteine-type endopeptidase activity
GO:2000308 negative regulation of tumor necrosis factor (ligand) superfamily member 11 production
GO:2001205 negative regulation of osteoclast development
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005769 early endosome
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0030141 secretory granule
GO:0032991 protein-containing complex
GO:0035580 specific granule lumen
GO:0042581 specific granule
GO:0055037 recycling endosome
GO:0070062 extracellular exosome
GO:0097013 phagocytic vesicle lumen
GO:1904724 tertiary granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1b0l, PDBe:1b0l, PDBj:1b0l
PDBsum1b0l
PubMed10089347
UniProtP02788|TRFL_HUMAN Lactotransferrin (Gene Name=LTF)

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