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 3-(1h-Indol-3-yl)-2-[4-(4-phenyl-piperidin-1-yl)-benzenesulfonylamino]-propionic acid Ligand Info
Canonical SMILES C1CN(CCC1C2=CC=CC=C2)C3=CC=C(C=C3)S(=O)(=O)NC(CC4=CNC5=CC=CC=C54)C(=O)O
InChI 1S/C28H29N3O4S/c32-28(33)27(18-22-19-29-26-9-5-4-8-25(22)26)30-36(34,35)24-12-10-23(11-13-24)31-16-14-21(15-17-31)20-6-2-1-3-7-20/h1-13,19,21,27,29-30H,14-18H2,(H,32,33)/t27-/m0/s1
InChIKey ULOTXPTWJAUGGE-MHZLTWQESA-N
PubChem Compound ID 444789
Drug Binding Sites of Target  Top
PDB ID: 1CIZ      X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXES WITH NON-PEPTIDE INHIBITORS: IMPLICATION FOR INHIBITOR SELECTIVITY
Method X-ray diffraction Resolution 1.64 Å 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
QSLYGPPP
Residue
Distance (Å)
PHE86
4.864
ASN162
3.958
VAL163
3.815
LEU164
2.786
ALA165
2.891
HIS166
3.808
ALA167
4.990
LEU197
3.704
VAL198
4.285
HIS201
3.430
GLU202
2.574
HIS205
3.351
PHE210
3.282
Residue
Distance (Å)
HIS211
3.304
GLU216
4.060
ALA217
3.479
LEU218
3.680
TYR220
3.145
PRO221
3.099
LEU222
3.376
TYR223
3.238
HIS224
3.337
SER225
4.770
LEU226
4.003
PHE232
3.726
PDB ID: 1CAQ      X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXES WITH NON-PEPTIDE INHIBITORS: IMPLICATION FOR INHIBITOR SELECTIVITY
Method X-ray diffraction Resolution 1.80 Å 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
QSLYGPPP
Residue
Distance (Å)
PHE86
3.937
ASN162
4.341
VAL163
3.884
LEU164
2.812
ALA165
2.726
HIS166
4.042
ALA167
3.313
LEU197
3.763
VAL198
4.176
HIS201
3.502
GLU202
2.642
HIS205
3.441
PHE210
3.636
Residue
Distance (Å)
HIS211
3.138
GLU216
4.345
ALA217
3.704
LEU218
3.793
TYR220
3.174
PRO221
3.307
LEU222
3.420
TYR223
3.598
HIS224
3.118
SER225
4.516
LEU226
3.712
PHE232
4.144
References  Top
REF 1 X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity. Protein Sci. 1999 Jul;8(7):1455-62.

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