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 T86702 Target Info
Target Name Matrix metalloproteinase-3 (MMP-3)
Synonyms Transin-1; Stromelysin-1; STMY1; SL-1; MMP-3
Target Type Patented-recorded Target
Gene Name MMP3
Biochemical Class Peptidase
UniProt ID
MMP3_HUMAN
Ligand General Information  Top
Ligand Name N-{(2r)-2-[2-(Hydroxyamino)-2-Oxoethyl]-4-Methylpentanoyl}-L-Leucyl-L-Phenylalaninamide Ligand Info
Canonical SMILES CC(C)CC(CC(=O)NO)C(=O)NC(CC(C)C)C(=O)NC(CC1=CC=CC=C1)C(=O)N
InChI 1S/C23H36N4O5/c1-14(2)10-17(13-20(28)27-32)22(30)26-19(11-15(3)4)23(31)25-18(21(24)29)12-16-8-6-5-7-9-16/h5-9,14-15,17-19,32H,10-13H2,1-4H3,(H2,24,29)(H,25,31)(H,26,30)(H,27,28)/t17-,18+,19+/m1/s1
InChIKey HLSQLCOADIMQBK-QYZOEREBSA-N
PubChem Compound ID 5496920
Drug Binding Sites of Target  Top
PDB ID: 1UMS      STROMELYSIN-1 CATALYTIC DOMAIN WITH HYDROPHOBIC INHIBITOR BOUND, PH 7.0, 32OC, 20 MM CACL2, 15% ACETONITRILE; NMR ENSEMBLE OF 20 STRUCTURES
Method Solution NMR Resolution N.A. Mutation No [1]
PDB Sequence
FRTFPGIPKW
92
RKTHLTYRIV
102
NYTPDLPKDA
112
VDSAVEKALK
122
VWEEVTPLTF
132

SRLYEGEADI
142
MISFAVREHG
152
DFYPFDGPGN
162
VLAHAYAPGP
172
GINGDAHFDD
182

DEQWTKDTTG
192
TNLFLVAAHE
202
IGHSLGLFHS
212
ANTEALMYPL
222
YHSLTDLTRF
232

RLSQDDINGI
242
QSLYGP
Residue
Distance (Å)
TYR155
2.398
PRO156
2.262
ASP158
3.215
GLY161
4.491
ASN162
2.006
VAL163
1.965
LEU164
3.333
ALA165
4.267
THR190
4.851
THR191
2.177
GLY192
3.053
THR193
4.537
LEU197
2.123
Residue
Distance (Å)
VAL198
3.698
ALA200
4.294
HIS201
2.201
HIS205
4.119
HIS211
3.288
LEU218
3.732
MET219
4.021
TYR220
3.689
PRO221
2.133
LEU222
1.943
TYR223
1.920
HIS224
2.338
SER225
4.670
PDB ID: 1UMT      Stromelysin-1 catalytic domain with hydrophobic inhibitor bound, ph 7.0, 32oc, 20 mm cacl2, 15% acetonitrile; nmr average of 20 structures minimized with restraints
Method Solution NMR Resolution N.A. Mutation No [1]
PDB Sequence
FRTFPGIPKW
92
RKTHLTYRIV
102
NYTPDLPKDA
112
VDSAVEKALK
122
VWEEVTPLTF
132

SRLYEGEADI
142
MISFAVREHG
152
DFYPFDGPGN
162
VLAHAYAPGP
172
GINGDAHFDD
182

DEQWTKDTTG
192
TNLFLVAAHE
202
IGHSLGLFHS
212
ANTEALMYPL
222
YHSLTDLTRF
232

RLSQDDINGI
242
QSLYGP
Residue
Distance (Å)
TYR155
2.439
ASP158
3.609
GLY161
4.370
ASN162
1.996
VAL163
1.903
LEU164
4.041
ALA165
4.620
THR191
2.216
GLY192
2.713
THR193
4.027
LEU197
2.209
VAL198
2.329
Residue
Distance (Å)
HIS201
2.441
HIS205
3.987
HIS211
2.338
LEU218
3.286
MET219
2.972
TYR220
2.416
PRO221
1.890
LEU222
1.997
TYR223
3.278
HIS224
4.603
SER225
4.869
References  Top
REF 1 Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor. Protein Sci. 1995 Dec;4(12):2487-98.

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