Structure of PDB 5lab Chain A Binding Site BS06

Receptor Information
>5lab Chain A (length=159) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINT
GMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADD
IRGIQSLYG
Ligand information
Ligand IDNGH
InChIInChI=1S/C13H20N2O5S/c1-10(2)8-15(9-13(16)14-17)21(18,19)12-6-4-11(20-3)5-7-12/h4-7,10,17H,8-9H2,1-3H3,(H,14,16)
InChIKeyJIRXORZYIXSWOB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)C[N@](CC(=O)NO)S(=O)(=O)c1ccc(cc1)OC
CACTVS 3.341COc1ccc(cc1)[S](=O)(=O)N(CC(C)C)CC(=O)NO
ACDLabs 10.04O=C(NO)CN(S(=O)(=O)c1ccc(OC)cc1)CC(C)C
OpenEye OEToolkits 1.5.0CC(C)CN(CC(=O)NO)S(=O)(=O)c1ccc(cc1)OC
FormulaC13 H20 N2 O5 S
NameN-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID
ChEMBLCHEMBL311932
DrugBankDB08271
ZINCZINC000003818629
PDB chain5lab Chain A Residue 306 [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]
PDB5lab Pseudo-Contact NMR Shifts over the Paramagnetic Metalloprotein CoMMP-12 from First Principles.
Resolution1.34 Å
Binding residue
(original residue number in PDB)		I180 A182 H218 E219 H222 H228 P238 Y240
Binding residue
(residue number reindexed from 1)		I76 A78 H114 E115 H118 H124 P134 Y136
Annotation score1
Binding affinityBindingDB: Ki=4.3nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H114 E115 H118 H124
Enzyme Commision number 3.4.24.65: macrophage elastase.
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:5lab, PDBe:5lab, PDBj:5lab
PDBsum5lab
PubMed
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

[Back to BioLiP]