Structure of PDB 6gcn Chain A

Receptor sequence
>6gcnA (length=418) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
MKVTFKDVAGIEEVKEEVKEIIEYLKDPVKFQPPKGVLLYGEPGVGKTLL
AKAIAGEAHVPFISVSGSDFVEMFVGVGAARVRDLFETAKKHAPCIIFID
EIDAVGRADEREQTLNQLLVEMDGFDTSDGIIVIAATNRPDILDPALLRP
GRFDRQIFIPKPDVRGRYEILKVHARNKKLAKDVDLEFVARATPGFTGAD
LENLLNEAALLAARKGKEEITMEEIEEALDRITMGKGMTISPKEKEKIAI
HEAGHALMGLVSDDDDKVHKISIIPRGKHIYDKKDLYNKILVLLGGRAAE
EVFFGKDGITTGAENDLQRATDLAYRMVSMWGMSDKVGPIAIRRTTAVDT
SPDLLREIDEEVKRIITEQYEKAKAIVEEYKEPLKAVVKKLLEKETITCE
EFVEVFKLYGIELKDKCK
3D structure
PDB6gcn Conformational flexibility of pore loop-1 gives insights into substrate translocation by the AAA+protease FtsH.
ChainA
Resolution2.949 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 A158 G198 V199 G200 K201 T202 L203 H338 G362 A363 E366 A9 G44 V45 G46 K47 T48 L49 H174 G198 A199 E202
BS02 ZN A H418 R443 D496 H251 R276 D316
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:6gcn, PDBe:6gcn, PDBj:6gcn
PDBsum6gcn
PubMed30118817
UniProtO67077|FTSH_AQUAE ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)

[Back to BioLiP]