Structure of PDB 5h52 Chain A
Receptor sequence
>5h52A (length=650) Species:
9606
(Homo sapiens) [
Search protein sequence
]
DKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAI
AANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVK
KDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVAN
FFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDV
AFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVV
ARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGF
LKVPPRMDAKMYLGYEYVTAIRNLREGTCPECKPVKWCALSHHERLKCDE
WSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPV
LAENYNAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLL
YNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGY
TGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGT
RKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNSETKDL
LFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP
3D structure
PDB
5h52
The role of citrate, lactate and transferrin in determining titanium release from surgical devices into human serum.
Chain
A
Resolution
3.0 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
?
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
4TI
A
D392 Y426 Y517 H585
D385 Y409 Y500 H568
BS02
4TI
A
A126 Y188
A124 Y186
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0008198
ferrous iron binding
GO:0008199
ferric iron binding
GO:0019899
enzyme binding
GO:0034986
iron chaperone activity
GO:0044325
transmembrane transporter binding
GO:0046872
metal ion binding
GO:1990459
transferrin receptor binding
Biological Process
GO:0006826
iron ion transport
GO:0006879
intracellular iron ion homeostasis
GO:0007015
actin filament organization
GO:0009617
response to bacterium
GO:0019731
antibacterial humoral response
GO:0030316
osteoclast differentiation
GO:0031647
regulation of protein stability
GO:0032436
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0034756
regulation of iron ion transport
GO:0042327
positive regulation of phosphorylation
GO:0045780
positive regulation of bone resorption
GO:0045893
positive regulation of DNA-templated transcription
GO:0048260
positive regulation of receptor-mediated endocytosis
GO:0060586
multicellular organismal-level iron ion homeostasis
GO:0070371
ERK1 and ERK2 cascade
GO:0071281
cellular response to iron ion
GO:2000147
positive regulation of cell motility
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005768
endosome
GO:0005769
early endosome
GO:0005770
late endosome
GO:0005788
endoplasmic reticulum lumen
GO:0005886
plasma membrane
GO:0005905
clathrin-coated pit
GO:0009925
basal plasma membrane
GO:0009986
cell surface
GO:0010008
endosome membrane
GO:0016020
membrane
GO:0016324
apical plasma membrane
GO:0030139
endocytic vesicle
GO:0030669
clathrin-coated endocytic vesicle membrane
GO:0031410
cytoplasmic vesicle
GO:0031982
vesicle
GO:0034774
secretory granule lumen
GO:0045178
basal part of cell
GO:0048471
perinuclear region of cytoplasm
GO:0055037
recycling endosome
GO:0070062
extracellular exosome
GO:0072562
blood microparticle
GO:1990712
HFE-transferrin receptor complex
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5h52
,
PDBe:5h52
,
PDBj:5h52
PDBsum
5h52
PubMed
29623422
UniProt
P02787
|TRFE_HUMAN Serotransferrin (Gene Name=TF)
[
Back to BioLiP
]