Structure of PDB 1ybq Chain B Binding Site BS03

Receptor Information
>1ybq Chain B (length=389) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIDYTAAGFTLLQGAHLYAPEDRGICDVLVANGKIIAVASNIPSDIVPNC
TVVDLSGQILCPGFIDQHVHLIGGGGEAGPTTRTPEVALSRLTEAGVTSV
VGLLGTDSISRHPESLLAKTRALNEEGISAWMLTGAYHVPSRTITGSVEK
DVAIIDRVIGVKCAISDHRSAAPDVYHLANMAAESRVGGLLGGKPGVTVF
HMGDSKKALQPIYDLLENCDVPISKLLPTHVNRNVPLFEQALEFARKGGT
IDITSSIDEPVAPAEGIARAVQAGIPLARVTLSSNGNGSQPFFDDEGNLT
HIGVAGFETLLETVQVLVKDYDFSISDALRPLTSSVAGFLNLTGKGEILP
GNDADLLVMTPELRIEQVYARGKLMVKDGKACVKGTFET
Ligand information
Ligand IDBDH
InChIInChI=1S/C10H14N4O5/c11-6(9(16)17)2-8(15)14-7(10(18)19)1-5-3-12-4-13-5/h3-4,6-7H,1-2,11H2,(H,12,13)(H,14,15)(H,16,17)(H,18,19)/t6-,7-/m0/s1
InChIKeyKABYBYFUSGXITA-BQBZGAKWSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c([nH]cn1)CC(C(=O)O)NC(=O)CC(C(=O)O)N
ACDLabs 10.04O=C(O)C(N)CC(=O)NC(C(=O)O)Cc1cncn1
OpenEye OEToolkits 1.5.0c1c([nH]cn1)C[C@@H](C(=O)O)NC(=O)C[C@@H](C(=O)O)N
CACTVS 3.341N[CH](CC(=O)N[CH](Cc1[nH]cnc1)C(O)=O)C(O)=O
CACTVS 3.341N[C@@H](CC(=O)N[C@@H](Cc1[nH]cnc1)C(O)=O)C(O)=O
FormulaC10 H14 N4 O5
NameL-BETA-ASPARTYLHISTIDINE
ChEMBL
DrugBank
ZINCZINC000002391076
PDB chain1ybq Chain B Residue 393 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ybq Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H70 G74 G75 T106 Y137 K162 R169 H201 R233 S289 P291
Binding residue
(residue number reindexed from 1)		H70 G74 G75 T106 Y137 K162 R169 H201 R233 S289 P291
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) H68 H70 K162 H201 H230 N285
Catalytic site (residue number reindexed from 1) H68 H70 K162 H201 H230 N285
Enzyme Commision number 3.4.19.-
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0008798 beta-aspartyl-peptidase 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ybq, PDBe:1ybq, PDBj:1ybq
PDBsum1ybq
PubMed15882050
UniProtP39377|IADA_ECOLI Isoaspartyl dipeptidase (Gene Name=iadA)

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