Structure of PDB 1pok Chain A

Receptor sequence

>1pokA (length=377) Species: 562 (Escherichia coli)

MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNC
TVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSV
VGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEK
DVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVF
HMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGT
IDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSDGNGSHIGVAGFETLL
ETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILPGNDADLLVMTP
ELRIEQVYARGKLMVKDGKACVKGTFE

3D structure

• PDB: 1pok X-ray structure of isoaspartyl dipeptidase from E.coli: a dinuclear zinc peptidase evolved from amidohydrolases.
• Chain: A
• Resolution: 2.7 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	A	H68 H70 K162 D285	H68 H70 K162 D285
BS02	ZN	A	K162 H201 H230	K162 H201 H230
BS03	ASN	A	R169 R233	R169 R233

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:1pok, PDBe:1pok, PDBj:1pok
• PDBsum: 1pok
• PubMed: 12946361
• UniProt: P39377|IADA_ECOLI Isoaspartyl dipeptidase (Gene Name=iadA)