Structure of PDB 2cea Chain A Binding Site BS01

Receptor Information

>2cea Chain A (length=406) Species: 2336 (Thermotoga maritima)

YKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILL
VGPPGTGKTLLARAVAGEANVPFFHISGSDFVELFVGVGAARVRDLFAQA
KAHAPCIVFIDEIDAVGRHDEREQTLNQLLVEMDGFDSKEGIIVMAATNR
PDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEII
AKRTPGFVGADLENLVNEAALLAAREGRDKITMKDFEEAIDRVILISPAE
KRIIAYHEAGHAVVSTVVPNGEPVHRISIIKYLVSRNELLDKLTALLGGR
AAEEVVFGDVTSGAANDIERATEIARNMVCQLGMSEELGPLAWGKLRNYS
EEVASKIDEEVKKIVTNCYERAKEIIRKYRKQLDNIVEILLEKETIEGDE
LRRILS

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2cea Chain A Residue 1603

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2cea The Molecular Architecture of the Metalloprotease Ftsh.
• Resolution: 2.75 Å
• Binding residue (original residue number in PDB): H423 H427 D500
• Binding residue (residue number reindexed from 1): H257 H261 D317
• 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

External links

• PDB: RCSB:2cea, PDBe:2cea, PDBj:2cea
• PDBsum: 2cea
• PubMed: 16484367
• UniProt: Q9WZ49|FTSH_THEMA ATP-dependent zinc metalloprotease FtsH (Gene Name=ftsH)