Structure of PDB 6tsj Chain AAA

Receptor sequence
>6tsjAAA (length=172) Species: 9606 (Homo sapiens) [Search protein sequence]
SQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFF
RELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMA
LEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNL
HRLGGPEAGLGEYLFERLTLKH
3D structure
PDB6tsj Iron Biomineral Growth from the Initial Nucleation Seed in L-Ferritin.
ChainAAA
Resolution2.3 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 FE AAA E57 E60 E61 E52 E55 E56
BS02 FE AAA E60 E64 E55 E59
BS03 FE AAA E61 E64 E56 E59
BS04 FE AAA E90 E92 E85 E87
BS05 FE AAA E57 E60 E52 E55
BS06 O AAA E60 E61 E64 E55 E56 E59
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008198 ferrous iron binding
GO:0008199 ferric iron binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006826 iron ion transport
GO:0006879 intracellular iron ion homeostasis
GO:0006880 intracellular sequestering of iron ion
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005776 autophagosome
GO:0005829 cytosol
GO:0016020 membrane
GO:0031410 cytoplasmic vesicle
GO:0035578 azurophil granule lumen
GO:0044754 autolysosome
GO:0070062 extracellular exosome
GO:0070288 ferritin complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6tsj, PDBe:6tsj, PDBj:6tsj
PDBsum6tsj
PubMed32027764
UniProtP02792|FRIL_HUMAN Ferritin light chain (Gene Name=FTL)

[Back to BioLiP]