Structure of PDB 1fls Chain A Binding Site BS04

Receptor Information
>1fls Chain A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDG
IADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS
SSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDV
QGIQSLYG
Ligand information
Ligand IDWAY
InChIInChI=1S/C21H21N3O5S/c1-15-5-3-7-19(21(25)23-26)20(15)24(14-16-6-4-12-22-13-16)30(27,28)18-10-8-17(29-2)9-11-18/h3-13,26H,14H2,1-2H3,(H,23,25)
InChIKeyAINJYWXKBKRQSX-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1ccc(cc1)[S](=O)(=O)N(Cc2cccnc2)c3c(C)cccc3C(=O)NO
ACDLabs 10.04O=C(NO)c3cccc(c3N(S(=O)(=O)c1ccc(OC)cc1)Cc2cccnc2)C
OpenEye OEToolkits 1.5.0Cc1cccc(c1N(Cc2cccnc2)S(=O)(=O)c3ccc(cc3)OC)C(=O)NO
FormulaC21 H21 N3 O5 S
NameN-HYDROXY-2-[(4-METHOXY-BENZENESULFONYL)-PYRIDIN-3-YLMETHYL-AMINO]-3-METHYL-BENZAMIDE;
WAY-151693
ChEMBLCHEMBL70176
DrugBankDB02071
ZINCZINC000000602968
PDB chain1fls Chain A Residue 169 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fls High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.
ResolutionN/A
Binding residue
(original residue number in PDB)		L81 H119 H123 H129 P139 Y141
Binding residue
(residue number reindexed from 1)		L75 H113 H117 H123 P133 Y135
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.48,IC50=33nM
BindingDB: IC50=8nM
Enzymatic activity
Catalytic site (original residue number in PDB) H119 E120 H123 H129
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.-
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0031012 extracellular matrix

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fls, PDBe:1fls, PDBj:1fls
PDBsum1fls
PubMed10986126
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

[Back to BioLiP]