Structure of PDB 2ce7 Chain A Binding Site BS01

Receptor Information
>2ce7 Chain A (length=406) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILL
VGPPGTGKTLLARAVAGEANVPFFHISGSDFVELFVGVGAARVRDLFAQA
KAHAPCIVFIDEIDAVGRHDEREQTLNQLLVEMDGFDSKEGIIVMAATNR
PDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEII
AKRTPGFVGADLENLVNEAALLAAREGRDKITMKDFEEAIDRVILISPAE
KRIIAYHEAGHAVVSTVVPNGEPVHRISIIKYLVSRNELLDKLTALLGGR
AAEEVVFGDVTSGAANDIERATEIARNMVCQLGMSEELGPLAWGKLRNYS
EEVASKIDEEVKKIVTNCYERAKEIIRKYRKQLDNIVEILLEKETIEGDE
LRRILS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2ce7 Chain A Residue 1603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2ce7 The Molecular Architecture of the Metalloprotease Ftsh.
Resolution2.44 Å
Binding residue
(original residue number in PDB)
H423 H427 D500
Binding residue
(residue number reindexed from 1)
H257 H261 D317
Annotation score1
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:2ce7, PDBe:2ce7, PDBj:2ce7
PDBsum2ce7
PubMed16484367
UniProtQ9WZ49|FTSH_THEMA ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)

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