Structure of PDB 1wm1 Chain A

Receptor sequence
>1wm1A (length=313) Species: 615 (Serratia marcescens) [Search protein sequence]
LRGLYPPLAAYDSGWLDTGDGHRIYWELSGNPNGKPAVFIHGGPGGGISP
HHRQLFDPERYKVLLFDQRGCGRSRPHASLDNNTTWHLVADIERLREMAG
VEQWLVFGGSWGSTLALAYAQTHPERVSEMVLRGIFTLRKQRLHWYYQDG
ASRFFPEKWERVLSILSDDERKDVIAAYRQRLTSADPQVQLEAAKLWSVW
EGETVTLLPSRESASFGEDDFALAFARIENHYFTHLGFLESDDQLLRNVP
LIRHIPAVIVHGRYDMACQVQNAWDLAKAWPEAELHIVEGAGHSYDEPGI
LHQLMIATDRFAG
3D structure
PDB1wm1 Novel inhibitor for prolyl aminopeptidase from Serratia marcescens and studies on the mechanism of substrate recognition of the enzyme using the inhibitor
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G46 S113 W114 D268 H296
Catalytic site (residue number reindexed from 1) G43 S110 W111 D265 H293
Enzyme Commision number 3.4.11.5: prolyl 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 PTB A G45 G46 S113 W114 R136 F139 E204 E232 F236 H296 G42 G43 S110 W111 R133 F136 E201 E229 F233 H293 MOAD: Ki=0.5uM
PDBbind-CN: -logKd/Ki=6.30,Ki=0.5uM
BindingDB: Ki=500nM
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1wm1, PDBe:1wm1, PDBj:1wm1
PDBsum1wm1
PubMed12893291
UniProtO32449|PIP_SERMA Proline iminopeptidase (Gene Name=pip)

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