Structure of PDB 6gco Chain A Binding Site BS02
Receptor Information
>6gco Chain A (length=409) Species:
224324
(Aquifex aeolicus VF5) [
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KVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQPPKGVLLYGEPGVGKTLLA
KAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFIDE
IDAVGRHDEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRPG
RFDRQIFIPKPDVRGRYEILKVHARNKKLAKDVDLEFVARATPGFTGADL
ENLLNEAALLAARKITMEEIEEALDRITMMTISPKEKEKIAIHEAGHALM
GLVSDDDDKVHKISIIPRGQLPIEDKHIYDKKDLYNKILVLLGGRAAEEV
FFGKDGITTGAENDLQRATDLAYRMVSMWGMSDKVGPIAITSPDLLREID
EEVKRIITEQYEKAKAIVEEYKEPLKAVVKKLLEKETITCEEFVEVFKLY
GIELKDKCK
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
6gco Chain A Residue 702 [
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Receptor-Ligand Complex Structure
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PDB
6gco
Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+protease FtsH.
Resolution
3.323 Å
Binding residue
(original residue number in PDB)
H418 H422 R443 D496
Binding residue
(residue number reindexed from 1)
H243 H247 R268 D314
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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Biological Process
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Cellular Component
External links
PDB
RCSB:6gco
,
PDBe:6gco
,
PDBj:6gco
PDBsum
6gco
PubMed
30118817
UniProt
O67077
|FTSH_AQUAE ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)
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