Structure of PDB 1txr Chain A Binding Site BS03

Receptor Information
>1txr Chain A (length=291) Species: 671 (Vibrio proteolyticus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MPPITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIA
SEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDS
TIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAA
EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
Ligand information
Ligand IDBES
InChIInChI=1S/C16H24N2O4/c1-10(2)8-13(16(21)22)18-15(20)14(19)12(17)9-11-6-4-3-5-7-11/h3-7,10,12-14,19H,8-9,17H2,1-2H3,(H,18,20)(H,21,22)/t12-,13+,14+/m1/s1
InChIKeyVGGGPCQERPFHOB-RDBSUJKOSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)C[C@@H](C(=O)O)NC(=O)[C@H]([C@@H](Cc1ccccc1)N)O
CACTVS 3.341CC(C)C[C@H](NC(=O)[C@@H](O)[C@H](N)Cc1ccccc1)C(O)=O
ACDLabs 10.04O=C(O)C(NC(=O)C(O)C(N)Cc1ccccc1)CC(C)C
OpenEye OEToolkits 1.5.0CC(C)CC(C(=O)O)NC(=O)C(C(Cc1ccccc1)N)O
CACTVS 3.341CC(C)C[CH](NC(=O)[CH](O)[CH](N)Cc1ccccc1)C(O)=O
FormulaC16 H24 N2 O4
Name2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC ACID;
BESTATIN
ChEMBLCHEMBL29292
DrugBankDB03424
ZINCZINC000001542895
PDB chain1txr Chain A Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1txr Spectroscopic and X-ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase from Aeromonas (Vibrio) proteolytica.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		D117 E151 E152 L155 D179 C223 Y225 C227 F244 F248 Y251 H256
Binding residue
(residue number reindexed from 1)		D117 E151 E152 L155 D179 C223 Y225 C227 F244 F248 Y251 H256
Annotation score3
Binding affinityMOAD: Ki=18nM
PDBbind-CN: -logKd/Ki=7.74,Ki=18nM
BindingDB: IC50=1.6nM,Ki=1.6nM
Enzymatic activity
Catalytic site (original residue number in PDB) H97 D117 E151 E152 D179 H256
Catalytic site (residue number reindexed from 1) H97 D117 E151 E152 D179 H256
Enzyme Commision number 3.4.11.10: bacterial leucyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0008235 metalloexopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1txr, PDBe:1txr, PDBj:1txr
PDBsum1txr
PubMed15274616
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

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