Structure of PDB 1qxw Chain A

Receptor sequence

>1qxwA (length=249) Species: 1280 (Staphylococcus aureus)

MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEY
GAISAPIHDENFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNG
YYADTGISFVVGESDDPMKQKVCDVATMAFENAIAKVKPGTKLSNIGKAV
HNTARQNDLKVIKNLTGHGVGLSLHEAPAHVLNYFDPKDKTLLTEGMVLA
IEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTKDGPILTTKI

3D structure

• PDB: 1qxw Crystal structures of staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate.
• Chain: A
• Resolution: 1.67 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D93 D104 H168 H175 E202 E233
• Catalytic site (residue number reindexed from 1): D93 D104 H168 H175 E202 E233
• Enzyme Commision number: 3.4.11.18: methionyl aminopeptidase.

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	CO	A	D104 H168 E202 E233	D104 H168 E202 E233
BS02	CO	A	D93 D104 E233	D93 D104 E233
BS03	M1C	A	C67 H76 D93 D104 H168 E202 F204 E233	C67 H76 D93 D104 H168 E202 F204 E233	MOAD: ic50=7uM PDBbind-CN: -logKd/Ki=5.15,IC50=7uM

Gene Ontology

Molecular Function

• GO:0004177 aminopeptidase activity
• GO:0004239 initiator methionyl aminopeptidase activity
• GO:0008235 metalloexopeptidase activity
• GO:0046872 metal ion binding
• GO:0046914 transition metal ion binding
• GO:0070006 metalloaminopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:1qxw, PDBe:1qxw, PDBj:1qxw
• PDBsum: 1qxw
• PubMed: 14998322
• UniProt: P0A078|MAP1_STAAM Methionine aminopeptidase (Gene Name=map)