Structure of PDB 1i6q Chain A

Receptor sequence
>1i6qA (length=689) Species: 9838 (Camelus dromedarius) [Search protein sequence]
ASKKSVRWCTTSPAESKKCAQWQRRMKKVRGPSVTCVKKTSRFECIQAIS
TEKADAVTLDGGLVYDAGLDPYKLRPIAAEVYGTENQPQTHYYAVAIAKK
GTNFQLNQLQGLKSCHTGLGRSAGWNIPMGLLRPFLDWTGPPEPLQKAVA
KFFSASCVPCVDGKEYPNLCQLCAGTGENKCACSSQEPYFGYSGAFKCLQ
DGAGDVAFVKDSTVFESLPAKADRDQYELLCPNNTRKPVDAFQECHLARV
PSHAVVARSVNGKEDLIWKLLVKAQEKFGRGKPSAFQLFGSPAGQKDLLF
KDSALGLLRIPKKIDSGLYLGSNYITAIRGLRETAAEVELRRAQVVWCAV
GSDEQLKCQEWSRQSNQSVVCATASTTEDCIALVLKGEADALSLDGGYIY
IAGKCGLVPVLAESQQSPESSGLDCVHRPVKGYLAVAVVRKANDKITWNS
LRGKKSCHTAVDRTAGWNIPMGPLFKDTDSCRFDEFFSQSCAPGSDPRSK
LCALCAGNEEGQLKCVPNSSERLYGYTGAFRCLAENVGDVAFVKDVTVLD
NTDGKGTEQWAKDLKLGDFELLCLNGTRKPVTEAESCHLPVAPNHAVVSR
IDKVAHLRQVLLRQQAHFGRNGEDCPGKFCLFQSKTKNLLFNDNTECLAK
LQGKTTYDEYLGPQYVTAIAKLRRCSTSPLLEACAFLMR
3D structure
PDB1i6q Protein intermediate trapped by the simultaneous crystallization process. Crystal structure of an iron-saturated intermediate in the Fe3+ binding pathway of camel lactoferrin at 2.7 a resolution.
ChainA
Resolution2.7 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 Y92 Y192 Y92 Y192
BS02 FE A R463 T464 Y526 R463 T464 Y526
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
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:0019731 antibacterial humoral response
GO:0019732 antifungal humoral response
GO:0031665 negative regulation of lipopolysaccharide-mediated signaling pathway
GO:0032680 regulation of tumor necrosis factor production
GO:0033690 positive regulation of osteoblast proliferation
GO:0043066 negative regulation of apoptotic process
GO:0045669 positive regulation of osteoblast differentiation
GO:0060349 bone morphogenesis
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: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:0005769 early endosome
GO:0005886 plasma membrane
GO:0042581 specific granule
GO:0055037 recycling endosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1i6q, PDBe:1i6q, PDBj:1i6q
PDBsum1i6q
PubMed11473113
UniProtQ9TUM0|TRFL_CAMDR Lactotransferrin (Gene Name=LTF)

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