Structure of PDB 2gg3 Chain A Binding Site BS03

Receptor Information
>2gg3 Chain A (length=263) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVN
EQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVI
KDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGA
AIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTF
TIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLR
KDDTIPAIISHDE
Ligand information
Ligand IDU13
InChIInChI=1S/C9H7FN6/c10-5-1-3-6(4-2-5)13-14-7-8(11)15-16-9(7)12/h1-4,11H,12H2/b11-8+,14-13+
InChIKeyHALOLQDLOLYIOW-ZOBWXTBZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[H]N=C1C(=C(N=N1)N)N=Nc2ccc(cc2)F
CACTVS 3.341NC1=C(N=Nc2ccc(F)cc2)C(=N)N=N1
OpenEye OEToolkits 1.5.0[H]/N=C/1\C(=C(N=N1)N)/N=N/c2ccc(cc2)F
ACDLabs 10.04Fc2ccc(/N=N/C=1C(=[N@H])N=NC=1N)cc2
FormulaC9 H7 F N6
Name4-(4-FLUORO-PHENYLAZO)-5-IMINO-5H-PYRAZOL-3-YLAMINE
ChEMBL
DrugBank
ZINC
PDB chain2gg3 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2gg3 Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		Y62 H63 H79 D97 D108 H171 F177 H178 E204 W221 E235
Binding residue
(residue number reindexed from 1)		Y61 H62 H78 D96 D107 H170 F176 H177 E203 W220 E234
Annotation score1
Binding affinityMOAD: ic50=0.58uM
PDBbind-CN: -logKd/Ki=6.24,IC50=0.58uM
BindingDB: IC50=580nM
Enzymatic activity
Catalytic site (original residue number in PDB) H79 D97 D108 H171 R175 H178 Q182 E204 N208 Q233 E235
Catalytic site (residue number reindexed from 1) H78 D96 D107 H170 R174 H177 Q181 E203 N207 Q232 E234
Enzyme Commision number 3.4.11.18: methionyl aminopeptidase.
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0004239 initiator methionyl aminopeptidase activity
GO:0008198 ferrous iron binding
GO:0008235 metalloexopeptidase activity
GO:0046872 metal ion binding
GO:0046914 transition metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2gg3, PDBe:2gg3, PDBj:2gg3
PDBsum2gg3
PubMed17120228
UniProtP0AE18|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

[Back to BioLiP]