Structure of PDB 1i6q Chain A Binding Site BS01

Receptor Information
>1i6q Chain A (length=689) Species: 9838 (Camelus dromedarius) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASKKSVRWCTTSPAESKKCAQWQRRMKKVRGPSVTCVKKTSRFECIQAIS
TEKADAVTLDGGLVYDAGLDPYKLRPIAAEVYGTENQPQTHYYAVAIAKK
GTNFQLNQLQGLKSCHTGLGRSAGWNIPMGLLRPFLDWTGPPEPLQKAVA
KFFSASCVPCVDGKEYPNLCQLCAGTGENKCACSSQEPYFGYSGAFKCLQ
DGAGDVAFVKDSTVFESLPAKADRDQYELLCPNNTRKPVDAFQECHLARV
PSHAVVARSVNGKEDLIWKLLVKAQEKFGRGKPSAFQLFGSPAGQKDLLF
KDSALGLLRIPKKIDSGLYLGSNYITAIRGLRETAAEVELRRAQVVWCAV
GSDEQLKCQEWSRQSNQSVVCATASTTEDCIALVLKGEADALSLDGGYIY
IAGKCGLVPVLAESQQSPESSGLDCVHRPVKGYLAVAVVRKANDKITWNS
LRGKKSCHTAVDRTAGWNIPMGPLFKDTDSCRFDEFFSQSCAPGSDPRSK
LCALCAGNEEGQLKCVPNSSERLYGYTGAFRCLAENVGDVAFVKDVTVLD
NTDGKGTEQWAKDLKLGDFELLCLNGTRKPVTEAESCHLPVAPNHAVVSR
IDKVAHLRQVLLRQQAHFGRNGEDCPGKFCLFQSKTKNLLFNDNTECLAK
LQGKTTYDEYLGPQYVTAIAKLRRCSTSPLLEACAFLMR
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain1i6q Chain A Residue 690 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		Y92 Y192
Binding residue
(residue number reindexed from 1)		Y92 Y192
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.21.-
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

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

[Back to BioLiP]