Structure of PDB 1x2e Chain A Binding Site BS01

Receptor Information
>1x2e Chain A (length=313) Species: 615 (Serratia marcescens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LRGLYPPLAAYDSGWLDTGDGHRIYWELSGNPNGKPAVFIHGGPGGGISP
HHRQLFDPERYKVLLFDQRGCGRSRPHASLDNNTTWHLVADIERLREMAG
VEQWLVFGGSWGSTLALAYAQTHPERVSEMVLRGIFTLRKQRLHWYYQDG
ASRFFPEKWERVLSILSDDERKDVIAAYRQRLTSADPQVQLEAAKLWSVW
EGETVTLLPSRESASFGEDDFALAFARIENHYFTHLGFLESDDQLLRNVP
LIRHIPAVIVHGRYDMACQVQNAWDLAKAWPEAELHIVEGAGHSYDEPGI
LHQLMIATDRFAG
Ligand information
Ligand IDATX
InChIInChI=1S/C9H15N3O2/c1-5(10)6(13)7-11-12-8(14-7)9(2,3)4/h5H,10H2,1-4H3/t5-/m0/s1
InChIKeyPVDZDTVFUVTTDU-YFKPBYRVSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(c1nnc(o1)C(C)(C)C)C(N)C
OpenEye OEToolkits 1.5.0C[C@@H](C(=O)c1nnc(o1)C(C)(C)C)N
CACTVS 3.341C[C@H](N)C(=O)c1oc(nn1)C(C)(C)C
OpenEye OEToolkits 1.5.0CC(C(=O)c1nnc(o1)C(C)(C)C)N
CACTVS 3.341C[CH](N)C(=O)c1oc(nn1)C(C)(C)C
FormulaC9 H15 N3 O2
Name(2S)-2-AMINO-1-(5-TERT-BUTYL-1,3,4-OXADIAZOL-2-YL)PROPAN-1-ONE;
2-ALANYL-5-TERT-BUTYL-[1,3,4]-OXADIAZOLE
ChEMBL
DrugBankDB07391
ZINC
PDB chain1x2e Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1x2e Unusual extra space at the active site and high activity for acetylated hydroxyproline of prolyl aminopeptidase from Serratia marcescens
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G45 G46 S113 W114 R136 F139 E204 H296
Binding residue
(residue number reindexed from 1)		G42 G43 S110 W111 R133 F136 E201 H293
Annotation score1
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.
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:1x2e, PDBe:1x2e, PDBj:1x2e
PDBsum1x2e
PubMed16452443
UniProtO32449|PIP_SERMA Proline iminopeptidase (Gene Name=pip)

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