Structure of PDB 3b3c Chain A Binding Site BS03

Receptor Information
>3b3c 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
EEVGLRGSQDLANQYKSEGKNVVSALQLDATNYKGSAQDVVFITDYTDSN
FTQYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFESKFND
YNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMGSATG
Ligand information
Ligand IDPLU
InChIInChI=1S/C5H14NO3P/c1-4(2)3-5(6)10(7,8)9/h4-5H,3,6H2,1-2H3,(H2,7,8,9)/t5-/m1/s1
InChIKeyHGCAUCAWEADMPM-RXMQYKEDSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(C)C[CH](N)[P](O)(O)=O
OpenEye OEToolkits 1.5.0CC(C)C[C@H](N)P(=O)(O)O
OpenEye OEToolkits 1.5.0CC(C)CC(N)P(=O)(O)O
CACTVS 3.341CC(C)C[C@H](N)[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)C(N)CC(C)C
FormulaC5 H14 N O3 P
NameLEUCINE PHOSPHONIC ACID
ChEMBLCHEMBL40422
DrugBankDB02386
ZINCZINC000002047807
PDB chain3b3c Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3b3c Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus.
Resolution1.46 Å
Binding residue
(original residue number in PDB)		H97 D117 E151 E152 D179 C227 Y251 H256
Binding residue
(residue number reindexed from 1)		H97 D117 E151 E152 D179 C227 Y251 H256
Annotation score1
Binding affinityMOAD: Ki=105uM
PDBbind-CN: -logKd/Ki=3.98,Ki=105uM
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:3b3c, PDBe:3b3c, PDBj:3b3c
PDBsum3b3c
PubMed18576673
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

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