Structure of PDB 1xrr Chain A

Receptor sequence
>1xrrA (length=290) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
ECIENYAKVNGIYIYYKLCKAPEEKAKLMTMHGGPGMSHDYLLSLRDMTK
EGITVLFYDQFGCGRSEEPDQSKFTIDYGVEEAEALRSKLFGNEKVFLMG
SSYGGALALAYAVKYQDHLKGLIVSGGLSSVPLTVKEMNRLIDELPAKYR
DAIKKYGSSGSYENPEYQEAVNYFYHQHLLRSEDWPPEVLKSLEYAERRN
VYRIMNGPNEFTITGTIKDWDITDKISAIKIPTLITVGEYDQVTPNVARV
IHEKIAGSELHVFRDCSHLTMWEDREGYNKLLSDFILKHL
3D structure
PDB1xrr X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 PRO A G37 S105 N209 E213 I216 G34 S102 N206 E210 I213
BS02 PRO A Y205 N212 Y202 N209
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:1xrr, PDBe:1xrr, PDBj:1xrr
PDBsum1xrr
PubMed15994304
UniProtP96084|PIP_THEAC Proline iminopeptidase (Gene Name=pip)

[Back to BioLiP]