Structure of PDB 1igb Chain A Binding Site BS03

Receptor Information
>1igb 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 IDIPO
InChIInChI=1S/C9H11IN2O2/c10-7-3-1-6(2-4-7)5-8(11)9(13)12-14/h1-4,8,14H,5,11H2,(H,12,13)/t8-/m1/s1
InChIKeyAJEPKWPHKPETBM-MRVPVSSYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1C[C@H](C(=O)NO)N)I
CACTVS 3.341N[C@H](Cc1ccc(I)cc1)C(=O)NO
OpenEye OEToolkits 1.5.0c1cc(ccc1CC(C(=O)NO)N)I
CACTVS 3.341N[CH](Cc1ccc(I)cc1)C(=O)NO
ACDLabs 10.04Ic1ccc(cc1)CC(C(=O)NO)N
FormulaC9 H11 I N2 O2
NamePARA-IODO-D-PHENYLALANINE HYDROXAMIC ACID
ChEMBL
DrugBankDB01980
ZINCZINC000006707115
PDB chain1igb Chain A Residue 520 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1igb The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D117 E151 E152 D179 C223 C227 F244 F248 Y251 H256
Binding residue
(residue number reindexed from 1)		D117 E151 E152 D179 C223 C227 F244 F248 Y251 H256
Annotation score1
Binding affinityMOAD: Ki=0.4uM
PDBbind-CN: -logKd/Ki=6.40,Ki=0.4uM
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

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1igb, PDBe:1igb, PDBj:1igb
PDBsum1igb
PubMed8647077
UniProtQ01693|AMPX_VIBPR Bacterial leucyl aminopeptidase

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