Structure of PDB 1onx Chain B

Receptor sequence

>1onxB (length=389) Species: 562 (Escherichia coli)

MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNC
TVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSV
VGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEK
DVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVF
HMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGT
IDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSQPFFDDEGNLT
HIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILP
GNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFET

3D structure

• PDB: 1onx High Resolution X-ray Structure of Isoaspartyl Dipeptidase from Escherichia coli
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H68 H70 K162 H201 H230 D285
• Catalytic site (residue number reindexed from 1): H68 H70 K162 H201 H230 D285
• Enzyme Commision number: 3.4.19.-

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	ZN	B	H68 H70 K162 D285	H68 H70 K162 D285
BS02	ZN	B	K162 H201 H230	K162 H201 H230
BS03	ASP	B	G74 G75 Y137 K162 H201 D285 S289	G74 G75 Y137 K162 H201 D285 S289

Gene Ontology

Molecular Function

• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding
• GO:0008798 beta-aspartyl-peptidase activity
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1onx, PDBe:1onx, PDBj:1onx
• PDBsum: 1onx
• PubMed: 12718528
• UniProt: P39377|IADA_ECOLI Isoaspartyl dipeptidase (Gene Name=iadA)