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Receptor Information

>2gg0 Chain A (length=262) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNE
QHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIK
DGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAA
IQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFT
IEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRK
DDTIPAIISHDE

Ligand ID

U11

InChI

InChI=1S/C16H20F3N3O5/c1-8(14(25)21-7-11(23)27-2)22-15(26)13(24)12(20)9-3-5-10(6-4-9)16(17,18)19/h3-6,8,12-13,24H,7,20H2,1-2H3,(H,21,25)(H,22,26)/t8-,12+,13-/m0/s1

InChIKey

KTNRONBAQGRLNO-CKLFPEKLSA-N

SMILES

Software	SMILES
ACDLabs 10.04	FC(F)(F)c1ccc(cc1)C(N)C(O)C(=O)NC(C(=O)NCC(=O)OC)C
OpenEye OEToolkits 1.5.0	C[C@@H](C(=O)NCC(=O)OC)NC(=O)[C@H]([C@@H](c1ccc(cc1)C(F)(F)F)N)O
CACTVS 3.341	COC(=O)CNC(=O)[CH](C)NC(=O)[CH](O)[CH](N)c1ccc(cc1)C(F)(F)F
CACTVS 3.341	COC(=O)CNC(=O)[C@H](C)NC(=O)[C@@H](O)[C@H](N)c1ccc(cc1)C(F)(F)F
OpenEye OEToolkits 1.5.0	CC(C(=O)NCC(=O)OC)NC(=O)C(C(c1ccc(cc1)C(F)(F)F)N)O

Formula

C16 H20 F3 N3 O5

Name

METHYL N-{(2S,3R)-3-AMINO-2-HYDROXY-3-[4-(TRIFLUOROMETHYL)PHENYL]PROPANOYL}ALANYLGLYCINATE;
{2-[3-AMINO-2-HYDROXY-3-(4-TRIFLUOROMETHYL-PHENYL)-PROPIONYLAMINO]-PROPIONYLAMINO}-ACETIC ACID METHYL ESTER

PDB chain

2gg0 Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2gg0 Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.
Resolution	1.28 Å
Binding residue (original residue number in PDB)	Y62 H79 D97 D108 Y168 H171 F177 H178 E204 E235
Binding residue (residue number reindexed from 1)	Y60 H77 D95 D106 Y166 H169 F175 H176 E202 E233
Annotation score	1
Binding affinity	MOAD: ic50=1.7uM PDBbind-CN: -logKd/Ki=5.77,IC50=1.7uM BindingDB: IC50=1700nM

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)	H77 D95 D106 H169 R173 H176 Q180 E202 N206 Q231 E233
Enzyme Commision number	3.4.11.18: methionyl aminopeptidase.

	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

PDB	RCSB:2gg0, PDBe:2gg0, PDBj:2gg0
PDBsum	2gg0
PubMed	17120228
UniProt	P0AE18\|MAP1_ECOLI Methionine aminopeptidase (Gene Name=map)

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Structure of PDB 2gg0 Chain A Binding Site BS03