Structure of PDB 1mu0 Chain A

Receptor sequence
>1mu0A (length=293) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
MDQECIENYAKVNGIYIYYKLCKAPEEKAKLMTMHGGPGMSHDYLLSLRD
MTKEGITVLFYDQFGCGRSEEPDQSKFTIDYGVEEAEALRSKLFGNEKVF
LMGSSYGGALALAYAVKYQDHLKGLIVSGGLSSVPLTVKEMNRLIDELPA
KYRDAIKKYGSSGSYENPEYQEAVNYFYHQHLLRSEDWPPEVLKSLEYAE
RRNVYRIMNGPNEFTITGTIKDWDITDKISAIKIPTLITVGEYDEVTPNV
ARVIHEKIAGSELHVFRDCSHLTMWEDREGYNKLLSDFILKHL
3D structure
PDB1mu0 Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism
ChainA
Resolution2.4 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) G37 S105 Y106 D244 H271
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 S105 Y106 M141 E213 H271 G36 G37 S105 Y106 M141 E213 H271
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1mu0, PDBe:1mu0, PDBj:1mu0
PDBsum1mu0
PubMed12374735
UniProtP96084|PIP_THEAC Proline iminopeptidase (Gene Name=pip)

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