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 [(4S)-5-anilino-4-[[(2S)-2-[[(1R)-1-carboxyethyl]amino]-4-phenylbutanoyl]amino]-5-oxopentyl]-(diaminomethylidene)azanium Ligand Info
Canonical SMILES CC(C(=O)O)NC(CCC1=CC=CC=C1)C(=O)NC(CCC[NH+]=C(N)N)C(=O)NC2=CC=CC=C2
InChI 1S/C25H34N6O4/c1-17(24(34)35)29-21(15-14-18-9-4-2-5-10-18)23(33)31-20(13-8-16-28-25(26)27)22(32)30-19-11-6-3-7-12-19/h2-7,9-12,17,20-21,29H,8,13-16H2,1H3,(H,30,32)(H,31,33)(H,34,35)(H4,26,27,28)/p+1/t17-,20+,21+/m1/s1
InChIKey HDGWGGCPTVXRNA-QMMLZNLJSA-O
PubChem Compound ID 5288637
Drug Binding Sites of Target  Top
PDB ID: 2SRT      CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR
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
QSLYGPPPDS
252
PET
Residue
Distance (Å)
GLY161
3.071
ASN162
2.210
VAL163
2.215
LEU164
1.797
ALA165
1.851
HIS166
2.544
ALA167
4.294
GLU184
4.212
THR193
4.534
LEU197
2.117
VAL198
2.085
ALA199
4.959
HIS201
2.598
Residue
Distance (Å)
GLU202
4.539
HIS205
3.761
HIS211
2.568
ALA217
3.827
LEU218
2.422
MET219
4.601
TYR220
2.271
PRO221
3.166
LEU222
2.279
TYR223
2.729
HIS224
3.012
PHE232
4.505
PDB ID: 1SLN      CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842
Method X-ray diffraction Resolution 2.27 Å Mutation No [2]
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)
GLY161
4.604
ASN162
1.975
VAL163
3.736
LEU164
1.838
ALA165
2.164
HIS166
4.345
LEU197
3.603
VAL198
3.582
HIS201
2.758
Residue
Distance (Å)
GLU202
1.824
HIS205
2.889
HIS211
2.983
LEU218
3.458
TYR220
3.561
PRO221
2.887
LEU222
3.575
TYR223
1.941
HIS224
4.653
References  Top
REF 1 The NMR structure of the inhibited catalytic domain of human stromelysin-1. Nat Struct Biol. 1994 Feb;1(2):111-8.
REF 2 Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci. 1995 Oct;4(10):1966-76.

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