Structure of PDB 6gco Chain A

Receptor sequence
>6gcoA (length=409) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
KVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQPPKGVLLYGEPGVGKTLLA
KAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFIDE
IDAVGRHDEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRPG
RFDRQIFIPKPDVRGRYEILKVHARNKKLAKDVDLEFVARATPGFTGADL
ENLLNEAALLAARKITMEEIEEALDRITMMTISPKEKEKIAIHEAGHALM
GLVSDDDDKVHKISIIPRGQLPIEDKHIYDKKDLYNKILVLLGGRAAEEV
FFGKDGITTGAENDLQRATDLAYRMVSMWGMSDKVGPIAITSPDLLREID
EEVKRIITEQYEKAKAIVEEYKEPLKAVVKKLLEKETITCEEFVEVFKLY
GIELKDKCK
3D structure
PDB6gco Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+protease FtsH.
ChainA
Resolution3.323 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 3.4.24.-
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 ADP A G198 V199 G200 K201 T202 H338 G362 A363 G43 V44 G45 K46 T47 H173 G197 A198
BS02 ZN A H418 H422 R443 D496 H243 H247 R268 D314
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6gco, PDBe:6gco, PDBj:6gco
PDBsum6gco
PubMed30118817
UniProtO67077|FTSH_AQUAE ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)

[Back to BioLiP]