Structure of PDB 5d3c Chain A Binding Site BS06

Receptor Information
>5d3c 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
THSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYAYVDINTFRLSADD
IRGIQSLYG
Ligand information
Ligand ID56O
InChIInChI=1S/C30H32ClN5O10/c31-20-3-1-2-18(12-20)16-4-6-17(7-5-16)24-15-21(46-36-24)13-19(14-25(37)35-45)29(43)34-23(9-11-27(40)41)30(44)33-22(28(32)42)8-10-26(38)39/h1-7,12,15,19,22-23,45H,8-11,13-14H2,(H2,32,42)(H,33,44)(H,34,43)(H,35,37)(H,38,39)(H,40,41)/t19-,22+,23+/m1/s1
InChIKeyVBMQORMYXJZHKU-OIBXWCBGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.9.2c1cc(cc(c1)Cl)c2ccc(cc2)c3cc(on3)CC(CC(=O)NO)C(=O)NC(CCC(=O)O)C(=O)NC(CCC(=O)O)C(=O)N
ACDLabs 12.01c2cc(c1cc(CC(C(NC(C(NC(CCC(O)=O)C(=O)N)=O)CCC(O)=O)=O)CC(NO)=O)on1)ccc2c3cccc(c3)Cl
OpenEye OEToolkits 1.9.2c1cc(cc(c1)Cl)c2ccc(cc2)c3cc(on3)C[C@H](CC(=O)NO)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N
CACTVS 3.385NC(=O)[CH](CCC(O)=O)NC(=O)[CH](CCC(O)=O)NC(=O)[CH](CC(=O)NO)Cc1onc(c1)c2ccc(cc2)c3cccc(Cl)c3
CACTVS 3.385NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](CC(=O)NO)Cc1onc(c1)c2ccc(cc2)c3cccc(Cl)c3
FormulaC30 H32 Cl N5 O10
NameN-[(2R)-2-{[3-(3'-chlorobiphenyl-4-yl)-1,2-oxazol-5-yl]methyl}-4-(hydroxyamino)-4-oxobutanoyl]-L-alpha-glutamyl-L-alpha-glutamine
ChEMBLCHEMBL4096462
DrugBank
ZINCZINC000584905166
PDB chain5d3c Chain A Residue 306 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5d3c Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played by the Zinc-Binding Group on Potency and Selectivity.
Resolution1.314 Å
Binding residue
(original residue number in PDB)		G178 G179 I180 L181 A182 T215 H218 E219 H222 H228 K233 V235 P238 T239 Y240 F248
Binding residue
(residue number reindexed from 1)		G74 G75 I76 L77 A78 T111 H114 E115 H118 H124 K129 V131 P134 T135 Y136 F144
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=10.40,Kd=40pM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5d3c, PDBe:5d3c, PDBj:5d3c
PDBsum5d3c
PubMed27996256
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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