Structure of PDB 3kds Chain E Binding Site BS01
Receptor Information
>3kds Chain E (length=427) Species:
2336
(Thermotoga maritima) [
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KRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGT
GATLLARAVAGEANVPFFHISGSDFVELFVGVGAARVRDLFAQAKAHAPC
IVFIDEIDAVGRHDEREQTLNQLLVEMDGFDSKEGIIVMAATNRPDILDP
ALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPG
FVGADLENLVNEAALLAAREGRDKITMKDFEEAIDRVIAGPARKSLLISP
AEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEEDK
YLVSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVCQ
LGMSEELGPLAWGKRLRNYSEEVASKIDEEVKKIVTNCYERAKEIIRKYR
KQLDNIVEILLEKETIEGDELRRILSE
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
3kds Chain E Residue 996 [
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Receptor-Ligand Complex Structure
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PDB
3kds
The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation
Resolution
2.601 Å
Binding residue
(original residue number in PDB)
H423 H427 D500
Binding residue
(residue number reindexed from 1)
H259 H263 D336
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.4.24.-
Gene Ontology
Molecular Function
GO:0004176
ATP-dependent peptidase activity
GO:0004222
metalloendopeptidase activity
GO:0005524
ATP binding
GO:0016887
ATP hydrolysis activity
Biological Process
GO:0006508
proteolysis
Cellular Component
GO:0016020
membrane
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Molecular Function
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Cellular Component
External links
PDB
RCSB:3kds
,
PDBe:3kds
,
PDBj:3kds
PDBsum
3kds
PubMed
19955424
UniProt
Q9WZ49
|FTSH_THEMA ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)
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