Structure of PDB 1sqy Chain A

Receptor sequence
>1sqyA (length=691) Species: 9606 (Homo sapiens) [Search protein sequence]
GRRRSVQWCTVSNPEATKCFQWQRNMRRVRGPPVSCVKRDSPTQCIQAIA
ENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKK
GGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVA
RFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLR
DGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARV
PSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPAFQLFGSPSGQKDLLF
KDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAV
GEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVY
TAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTW
NSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGRDPR
SNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTV
LQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVV
SRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECL
ARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
3D structure
PDB1sqy Structure of human diferric lactoferrin at 2.5A resolution using crystals grown at pH 6.5.
ChainA
Resolution2.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D395 Y435 Y528 H597 D395 Y435 Y528 H597
BS02 FE A D60 Y92 Y192 H253 D60 Y92 Y192 H253
BS03 CO3 A D60 T117 R121 T122 A123 Y192 D60 T117 R121 T122 A123 Y192
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1sqy, PDBe:1sqy, PDBj:1sqy
PDBsum1sqy
PubMed
UniProtP02788|TRFL_HUMAN Lactotransferrin (Gene Name=LTF)

[Back to BioLiP]