Structure of PDB 1utz Chain B Binding Site BS01

Receptor Information
>1utz Chain B (length=159) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTG
MADILVVFARGAHGDFHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTT
HSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDI
RGIQSLYGD
Ligand information
Ligand IDPF3
InChIInChI=1S/C25H20N2O3S/c28-24(29)15-22(20-4-2-1-3-5-20)27-25(30)23-14-21(16-31-23)18-8-6-17(7-9-18)19-10-12-26-13-11-19/h1-14,16,22H,15H2,(H,27,30)(H,28,29)/t22-/m1/s1
InChIKeyVMTJQZUZINLEKC-JOCHJYFZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(cc1)C(CC(=O)O)NC(=O)c2cc(cs2)c3ccc(cc3)c4ccncc4
CACTVS 3.341OC(=O)C[C@@H](NC(=O)c1scc(c1)c2ccc(cc2)c3ccncc3)c4ccccc4
OpenEye OEToolkits 1.5.0c1ccc(cc1)[C@@H](CC(=O)O)NC(=O)c2cc(cs2)c3ccc(cc3)c4ccncc4
ACDLabs 10.04O=C(O)CC(c1ccccc1)NC(=O)c4scc(c3ccc(c2ccncc2)cc3)c4
CACTVS 3.341OC(=O)C[CH](NC(=O)c1scc(c1)c2ccc(cc2)c3ccncc3)c4ccccc4
FormulaC25 H20 N2 O3 S
Name(2R)-3-({[4-[(PYRIDIN-4-YL)PHENYL]-THIEN-2-YL}CARBOXAMIDO)(PHENYL)PROPANOIC ACID;
PF-00356231;
3-PHENYL-3-({[4-(4-PYRIDIN-4-YLPHENYL)THIEN-2-YL]CARBONYL}AMINO)PROPANOIC ACID
ChEMBLCHEMBL508461
DrugBankDB03367
ZINCZINC000006744035
PDB chain1utz Chain A Residue 1266 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1utz Crystal Structures of Novel Non-Peptidic, Non-Zinc Chelating Inhibitors Bound to Mmp-12
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D175 K177 G179 P238
Binding residue
(residue number reindexed from 1)		D70 K72 G74 P133
Annotation score1
Binding affinityMOAD: ic50=0.014uM
PDBbind-CN: -logKd/Ki=5.85,IC50=1.4uM
BindingDB: IC50=14nM
Enzymatic activity
Catalytic site (original residue number in PDB) H218 E219 H222 H228
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1utz, PDBe:1utz, PDBj:1utz
PDBsum1utz
PubMed15289103
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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