Structure of PDB 3k1l Chain A Binding Site BS02
Receptor Information
>3k1l Chain A (length=376) Species:
7227
(Drosophila melanogaster) [
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EDVERLLCQKYPGLAAELQPSGACIIRGVLGSEDTWRRLKLYLPHHPALH
GFQLYVQESLEYKLYTSANLKLQDDWLLEDFLDHLPKILPAQKAPTVPEL
CREGNIYYDILALYKSNEYCLQVDEACSMIRFSEFTDFEQHYLELKIPSL
LLLDHSLPDCVSLGEMLTKSAGNLEEALNLFRKLLEDLRPFYDNFMDIDE
LCHVLQPSPISSKHKTRLFPLKDRVYLKLTIADPFACIASMSLKIIGPTE
EVARLRHVLSDGLSNWDSEMNIHKNLLRMFDLCYFPMPDWSDGPKLDEED
NEELRCNICFAYRLDGGEVPLVSCDNAKCVLKCHAVCLEEWFKTLMDGKT
FLEVSFGQCPFCKAKLSTSFAALLND
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
3k1l Chain A Residue 382 [
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Receptor-Ligand Complex Structure
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PDB
3k1l
The structure of the catalytic subunit FANCL of the Fanconi anemia core complex
Resolution
3.2 Å
Binding residue
(original residue number in PDB)
C329 C334 C364 C367
Binding residue
(residue number reindexed from 1)
C324 C329 C359 C362
Annotation score
4
Enzymatic activity
Enzyme Commision number
2.3.2.27
: RING-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0004842
ubiquitin-protein transferase activity
GO:0016740
transferase activity
GO:0046872
metal ion binding
GO:0061630
ubiquitin protein ligase activity
Biological Process
GO:0006281
DNA repair
GO:0006513
protein monoubiquitination
GO:0016567
protein ubiquitination
GO:0036297
interstrand cross-link repair
Cellular Component
GO:0005575
cellular_component
GO:0005634
nucleus
GO:0043240
Fanconi anaemia nuclear complex
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:3k1l
,
PDBe:3k1l
,
PDBj:3k1l
PDBsum
3k1l
PubMed
20154706
UniProt
Q8T913
|FANCL_DROME E3 ubiquitin-protein ligase Fancl (Gene Name=Fancl)
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