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 T42881 Target Info
Target Name Cytomegalovirus Protease (CMV UL80)
Synonyms UL80; Capsid protein P40; Assemblin
Target Type Patented-recorded Target
Gene Name CMV UL80
Biochemical Class Peptidase
UniProt ID
SCAF_HCMVA
Ligand General Information  Top
Ligand Name N-(6-Aminohexanoyl)-3-Methyl-L-Valyl-3-Methyl-L-Valyl-N~1~-[(2s,3s)-3-Hydroxy-4-Oxo-4-{[(1r)-1-Phenylpropyl]amino}butan-2-Yl]-N~4~,N~4~-Dimethyl-L-Aspartamide Ligand Info
Canonical SMILES CCC(C1=CC=CC=C1)NC(=O)C(C(C)NC(=O)C(CC(=O)N(C)C)NC(=O)C(C(C)(C)C)NC(=O)C(C(C)(C)C)NC(=O)CCCCCN)O
InChI 1S/C37H63N7O7/c1-11-25(24-18-14-12-15-19-24)40-33(49)29(47)23(2)39-32(48)26(22-28(46)44(9)10)41-34(50)31(37(6,7)8)43-35(51)30(36(3,4)5)42-27(45)20-16-13-17-21-38/h12,14-15,18-19,23,25-26,29-31,47H,11,13,16-17,20-22,38H2,1-10H3,(H,39,48)(H,40,49)(H,41,50)(H,42,45)(H,43,51)/t23-,25+,26-,29-,30+,31+/m0/s1
InChIKey RICYNZHPHSJRNO-GYZAPQSVSA-N
PubChem Compound ID 23585980
Drug Binding Sites of Target  Top
PDB ID: 1NJU      Complex structure of HCMV Protease and a peptidomimetic inhibitor
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [1]
PDB Sequence
DEQQSQAVAP
13
VYVGGFLARY
23
DQSPDEAELL
33
LPRDVVEHWL
43
HAQLSVALPL
59

NINHDDTAVV
69
GHVAAMQSVR
79
DGLFCLGCVT
89
SPRFLEIVRR
99
ASEKSELVSR
109

GPVSPLQPDK
119
VVEFLSGSYA
129
GLSLSSRRCD
139
DVEQTTPFKH
157
VALCSVGRRR
167

GTLAVYGRDP
177
EWVTQRFPDL
187
TAADRDGLRA
197
QWQSGDPFRS
216
DSYGLLGNSV
226

DALYIRERLP
236
KLRYDKQLVG
246
VTERESYVKA
256
Residue
Distance (Å)
GLU31
3.369
LEU32
3.712
ASN62
3.547
HIS63
2.827
LEU131
3.977
SER132
1.439
LEU133
3.064
SER134
2.730
SER135
2.737
ARG136
3.174
ARG137
2.698
Residue
Distance (Å)
LYS156
4.973
HIS157
4.401
CYS161
3.376
SER162
4.753
VAL163
3.096
GLY164
3.407
ARG165
2.854
ARG166
3.546
ILE231
3.343
LYS237
4.967
PDB ID: 1NKM      Complex structure of HCMV Protease and a peptidomimetic inhibitor
Method X-ray diffraction Resolution 2.70 Å Mutation Yes [1]
PDB Sequence
DEQQSQAVAP
13
VYVGGFLARY
23
DQSPDEAELL
33
LPRDVVEHWL
43
HAQALPLNIN
62

HDDTAVVGHV
72
AAMQSVRDGL
82
FCLGCVTSPR
92
FLEIVRRASE
102
KSELVSRGPV
112

SPLQPDKVVE
122
FLSGSYAGLS
132
LSSRRTTPFK
156
HVALCSVGRR
166
RGTLAVYGRD
176

PEWVTQRFPD
186
LTAADRDGLR
196
AQWQGDPFRS
216
DSYGLLGNSV
226
DALYIRERLP
236

KLRYDKQLVG
246
VTERESYVKA
256
Residue
Distance (Å)
GLU31
3.882
LEU32
3.930
ASN62
3.045
HIS63
3.079
LEU131
4.312
SER132
1.443
LEU133
3.361
SER134
2.906
SER135
2.681
ARG136
3.156
Residue
Distance (Å)
ARG137
4.742
LYS156
2.749
HIS157
4.534
CYS161
3.157
SER162
4.880
VAL163
3.032
GLY164
3.386
ARG165
2.655
ARG166
4.060
ILE231
3.562
PDB ID: 1JQ7      HCMV protease dimer-interface mutant, S225Y complexed to Inhibitor BILC 408
Method X-ray diffraction Resolution 3.00 Å Mutation Yes [2]
PDB Sequence
QSQAVAPVYV
1016
GGFLARYDQS
1026
PDEAELLLPR
1036
DVVEHWLSVA
1056
LPLNINHDDT
1066

AVVGHVAAMQ
1076
SVRDGLFCLG
1086
CVTSPRFLEI
1096
VRRASEKSEL
1106
VSRGPVSPLQ
1116

PDKVVEFLSG
1126
SYAGLSLSSP
1154
FKHVALCSVG
1164
RRRGTLAVYG
1174
RDPEWVTQRF
1184

PDLTAADRDG
1194
LRAQWDPFRS
1216
DSYGLLGNYV
1226
DALYIRERLP
1236
KLRYDKQLVG
1246

VTERESYVKA
1256
Residue
Distance (Å)
GLU1031
3.502
LEU1032
4.407
ASN1062
2.876
HIS1063
2.203
LEU1131
4.325
SER1132
1.435
LEU1133
2.493
SER1134
2.676
SER1135
3.369
Residue
Distance (Å)
LYS1156
4.203
HIS1157
3.706
CYS1161
3.414
VAL1163
3.468
GLY1164
3.615
ARG1165
2.558
ARG1166
3.397
ILE1231
3.611
References  Top
REF 1 Structural and biochemical studies of inhibitor binding to human cytomegalovirus protease. Biochemistry. 2003 Feb 4;42(4):885-91.
REF 2 Molecular mechanism for dimerization to regulate the catalytic activity of human cytomegalovirus protease. Nat Struct Biol. 2001 Sep;8(9):810-7.

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