Structure of PDB 1xqw Chain A

Receptor sequence
>1xqwA (length=290) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
ECIENYAKVNGIYIYYKLCKAPEEKAKLMTMHGGPGMSHDYLLSLRDMTK
EGITVLFYDQFGCGRSEEPDQSKFTIDYGVEEAEALRSKLFGNEKVFLMG
SAYGGALALAYAVKYQDHLKGLIVSGGLSSVPLTVKEMNRLIDELPAKYR
DAIKKYGSSGSYENPEYQEAVNYFYHQHLLRSEDWPPEVLKSLEYAERRN
VYRIMNGPNEFTITGTIKDWDITDKISAIKIPTLITVGEYDEVTPNVARV
IHEKIAGSELHVFRDCSHLTMWEDREGYNKLLSDFILKHL
3D structure
PDB1xqw X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G37 A105 Y106 D244 H271
Catalytic site (residue number reindexed from 1) G34 A102 Y103 D241 H268
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 PHE A G37 A105 Y106 L131 V134 T137 E213 I216 G34 A102 Y103 L128 V131 T134 E210 I213
BS02 LEU A G36 M40 Y44 S104 A105 E213 H271 G33 M37 Y41 S101 A102 E210 H268
BS03 PHE A Q171 V174 Y178 L196 Q168 V171 Y175 L193
BS04 LEU A Q171 Y178 L196 Q168 Y175 L193
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1xqw, PDBe:1xqw, PDBj:1xqw
PDBsum1xqw
PubMed15994304
UniProtP96084|PIP_THEAC Proline iminopeptidase (Gene Name=pip)

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