Structure of PDB 830c Chain A Binding Site BS04

Receptor Information
>830c Chain A (length=164) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTFMLPDD
DVQGIQSLYGPGDE
Ligand information
Ligand IDRS1
InChIInChI=1S/C19H20ClNO6S/c20-14-1-3-15(4-2-14)27-16-5-7-17(8-6-16)28(24,25)13-19(18(22)21-23)9-11-26-12-10-19/h1-8,23H,9-13H2,(H,21,22)
InChIKeyROSNVSQTEGHUKU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(ccc1Oc2ccc(cc2)Cl)S(=O)(=O)CC3(CCOCC3)C(=O)NO
CACTVS 3.341ONC(=O)C1(CCOCC1)C[S](=O)(=O)c2ccc(Oc3ccc(Cl)cc3)cc2
ACDLabs 10.04O=S(=O)(c2ccc(Oc1ccc(Cl)cc1)cc2)CC3(C(=O)NO)CCOCC3
FormulaC19 H20 Cl N O6 S
Name4-[4-(4-CHLORO-PHENOXY)-BENZENESULFONYLMETHYL]-TETRAHYDRO-PYRAN-4-CARBOXYLIC ACID HYDROXYAMIDE
ChEMBLCHEMBL440498
DrugBankDB08490
ZINCZINC000001488366
PDB chain830c Chain A Residue 1 [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]
PDB830c Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		L185 A186 H222 E223 H226 H232 L239 F241 I243 Y244
Binding residue
(residue number reindexed from 1)		L82 A83 H119 E120 H123 H129 L136 F138 I140 Y141
Annotation score1
Binding affinityMOAD: Ki=0.52nM
PDBbind-CN: -logKd/Ki=9.28,Ki=0.52nM
BindingDB: IC50=0.010000nM,Ki=0.52nM
Enzymatic activity
Catalytic site (original residue number in PDB) H222 E223 H226 H232
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
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:830c, PDBe:830c, PDBj:830c
PDBsum830c
PubMed10074939
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

[Back to BioLiP]