Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T85944 Target Info
Target Name Pseudomonas UDP-3-O-acyl-GlcNAc deacetylase (Pseudo lpxC)
Synonyms Pseudo UDP-3-O-acyl-GlcNAc deacetylase; EnvA protein
Target Type Preclinical Target
Gene Name Pseudo lpxC
Biochemical Class Carbon-nitrogen hydrolase
UniProt ID
LPXC_PSEAE
Ligand General Information  Top
Ligand Name N-[(1s,2r)-2-Hydroxy-1-(Hydroxycarbamoyl)propyl]-4-(4-Phenylbuta-1,3-Diyn-1-Yl)benzamide Ligand Info
Canonical SMILES CC(C(C(=O)NO)NC(=O)C1=CC=C(C=C1)C#CC#CC2=CC=CC=C2)O
InChI 1S/C21H18N2O4/c1-15(24)19(21(26)23-27)22-20(25)18-13-11-17(12-14-18)10-6-5-9-16-7-3-2-4-8-16/h2-4,7-8,11-15,19,24,27H,1H3,(H,22,25)(H,23,26)/t15-,19+/m1/s1
InChIKey VUYMSCCEGRLBAF-BEFAXECRSA-N
PubChem Compound ID 11164341
Drug Binding Sites of Target  Top
PDB ID: 4FW4      Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor
Method X-ray diffraction Resolution 2.19 Å Mutation Yes [1]
PDB Sequence
AMIKQRTLKN
9
IIRATGVGLH
19
SGEKVYLTLK
29
PAPVDTGIVF
39
SRTDLDPVVE
49

IPARAENVGE
59
TTMSTTLVKG
69
DVKVDTVEHL
79
LSAMAGLGID
89
NAYVELSASE
99

VPIMDGSAGP
109
FVFLIQSAGL
119
QEQEAAKKFI
129
RIKREVSVEE
139
GDKRAVFVPF
149

DGFKVSFEID
159
FDHPVFRGRT
169
QQASVDFSST
179
SFVKEVSRAR
189
TFGFMRDIEY
199

LRSQNLALGG
209
SVENAIVVDE
219
NRVLNEDGLR
229
YEDEFVKHKI
239
LDAIGDLYLL
249

GNSLIGEFRG
259
FKSGHALNNQ
269
LLRTLIADKD
279
AWEVVTFEDA
289
RTAPISYMRP
299
Residue
Distance (Å)
LEU18
4.028
HIS19
3.955
MET62
3.634
SER63
4.714
GLU77
2.370
HIS78
3.410
THR190
2.509
PHE191
2.971
GLY192
4.263
MET194
4.494
ILE197
3.639
LEU200
3.957
Residue
Distance (Å)
ARG201
4.008
ALA206
3.868
GLY209
3.476
SER210
3.617
VAL211
4.049
ALA214
3.781
VAL216
3.848
HIS237
2.799
LYS238
3.553
ASP241
2.893
HIS264
2.844
PDB ID: 3P3E      Crystal Structure of the PSEUDOMONAS AERUGINOSA LpxC/LPC-009 complex
Method X-ray diffraction Resolution 1.28 Å Mutation Yes [2]
PDB Sequence
MIKQRTLKNI
10
IRATGVGLHS
20
GEKVYLTLKP
30
APVDTGIVFS
40
RTDLDPVVEI
50

PARAENVGET
60
TMSTTLVKGD
70
VKVDTVEHLL
80
SAMAGLGIDN
90
AYVELSASEV
100

PIMDGSAGPF
110
VFLIQSAGLQ
120
EQEAAKKFIR
130
IKREVSVEEG
140
DKRAVFVPFD
150

GFKVSFEIDF
160
DHPVFRGRTQ
170
QASVDFSSTS
180
FVKEVSRART
190
FGFMRDIEYL
200

RSQNLALGGS
210
VENAIVVDEN
220
RVLNEDGLRY
230
EDEFVKHKIL
240
DAIGDLYLLG
250

NSLIGEFRGF
260
KSGHALNNQL
270
LRTLIADKDA
280
WEVVTFEDAR
290
TAPISYM
Residue
Distance (Å)
LEU18
3.012
HIS19
4.577
MET62
2.537
SER63
3.722
THR75
4.976
GLU77
2.570
HIS78
3.141
THR190
2.022
PHE191
3.224
GLY192
3.621
ILE197
2.871
LEU200
3.808
Residue
Distance (Å)
ARG201
3.237
ALA206
3.728
GLY209
2.894
SER210
2.774
VAL211
2.899
ALA214
3.307
VAL216
3.554
HIS237
2.889
LYS238
3.520
ASP241
2.851
HIS264
2.002
References  Top
REF 1 Crystal Structure of the LpxC in complex with N-[(1S,2R)-2-HYDROXY-1-(HYDROXYCARBAMOYL)PROPYL]-4-(4-PHENYLBUTA-1,3-DIYN-1-YL)BENZAMIDE inhibitor
REF 2 Species-specific and inhibitor-dependent conformations of LpxC: implications for antibiotic design. Chem Biol. 2011 Jan 28;18(1):38-47.

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