Structure of PDB 1xrl Chain A

Receptor sequence
>1xrlA (length=290) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
ECIENYAKVNGIYIYYKLCKAPEEKAKLMTMHGGPGMSHDYLLSLRDMTK
EGITVLFYDQFGCGRSEEPDQSKFTIDYGVEEAEALRSKLFGNEKVFLMG
SSYGGALALAYAVKYQDHLKGLIVSGGLSSVPLTVKEMNRLIDELPAKYR
DAIKKYGSSGSYENPEYQEAVNYFYHQHLLRSEDWPPEVLKSLEYAERRN
VFRIMNGPNEFTITGTIKDWDITDKISAIKIPTLITVGEYDEVTPNVARV
IHEKIAGSELHVFRDCSHLTMWEDREGYNKLLSDFILKHL
3D structure
PDB1xrl X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum
ChainA
Resolution1.82 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 S105 Y106 D244 H271
Catalytic site (residue number reindexed from 1) G34 S102 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 PHK A G36 G37 Y44 S105 Y106 M141 N209 E213 H271 G33 G34 Y41 S102 Y103 M138 N206 E210 H268
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1xrl, PDBe:1xrl, PDBj:1xrl
PDBsum1xrl
PubMed15994304
UniProtP96084|PIP_THEAC Proline iminopeptidase (Gene Name=pip)

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