Structure of PDB 1blf Chain A Binding Site BS02

Receptor Information
>1blf Chain A (length=685) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NVRWCTISQPEWFKCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKKA
DAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESPQTHYYAVAVVKKGSNF
QLDQLQGRKSCHTGLGRSAGWIIPMGILRPYLSWTESLEPLQGAVAKFFS
ASCVPCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYSGAFKCLQDGAG
DVAFVKETTVFENLPEKADRDQYELLCLNNSRAPVDAFKECHLAQVPSHA
VVARSVDGKEDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLLFKDSA
LGFLRIPSKVDSALYLGSRYLTTLKNLRETAEEVKARYTRVVWCAVGPEE
QKKCQQWSQQSGQNVTCATASTTDDCIVLVLKGEADALNLDGGYIYTAGK
CGLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKKANEGLTWNSLKDK
KSCHTAVDRTAGWNIPMGLIVNQTGSCAFDEFFSQSCAPGADPKSRLCAL
CAGDDQGLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKNDTVWENTNG
ESTADWAKNLNREDFRLLCLDGTRKPVTEAQSCHLAVAPNHAVVSRSDRA
AHVKQVLLHQQALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAKLGGR
PTYEEYLGTEYVTAIANLKKCSTSPLLEACAFLTR
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 chain1blf Chain A Residue 700 [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]
PDB1blf Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		D60 Y92 Y192 H253
Binding residue
(residue number reindexed from 1)		D56 Y88 Y188 H249
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.21.-
Gene Ontology
Molecular Function
GO:0004869 cysteine-type endopeptidase inhibitor activity
GO:0005102 signaling receptor binding
GO:0005515 protein binding
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:0042742 defense response to bacterium
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: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: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:1blf, PDBe:1blf, PDBj:1blf
PDBsum1blf
PubMed9398529
UniProtP24627|TRFL_BOVIN Lactotransferrin (Gene Name=LTF)

[Back to BioLiP]