Structure of PDB 1qxz Chain A

Receptor sequence
>1qxzA (length=249) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MIVKTEEELQALKEIGYICAKVRNTMQAATKPGITTKELDNIAKELFEEY
GAISAPIHDENFPGQTCISVNEEVAHGIPSKRVIREGDLVNIDVSALKNG
YYADTGISFVVGESDDPMKQKVCDVATMAFENAIAKVKPGTKLSNIGKAV
HNTARQNDLKVIKNLTGHGVGLSLHEAPAHVLNYFDPKDKTLLTEGMVLA
IEPFISSNASFVTEGKNEWAFETSDKSFVAQIEHTVIVTKDGPILTTKI
3D structure
PDB1qxz Crystal structures of staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate.
ChainA
Resolution1.68 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D97 D108 H171 H178 E204 E235
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 D108 H171 E204 E235 D104 H168 E202 E233
BS02 CO A D97 D108 E235 D93 D104 E233
BS03 CO A H171 H178 H168 H175
BS04 M3C A H79 D97 D108 H178 E204 F206 E235 H76 D93 D104 H175 E202 F204 E233 MOAD: ic50=19uM
PDBbind-CN: -logKd/Ki=4.72,IC50=19uM
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

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Molecular Function

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Biological Process
External links
PDB RCSB:1qxz, PDBe:1qxz, PDBj:1qxz
PDBsum1qxz
PubMed14998322
UniProtP0A078|MAP1_STAAM Methionine aminopeptidase (Gene Name=map)

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