Structure of PDB 5cxa Chain A Binding Site BS06

Receptor Information
>5cxa 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 ID55L
InChIInChI=1S/C30H31ClN4O10/c31-20-3-1-2-18(12-20)16-4-6-17(7-5-16)24-15-21(45-35-24)13-19(14-27(40)41)29(43)34-23(9-11-26(38)39)30(44)33-22(28(32)42)8-10-25(36)37/h1-7,12,15,19,22-23H,8-11,13-14H2,(H2,32,42)(H,33,44)(H,34,43)(H,36,37)(H,38,39)(H,40,41)/t19-,22+,23+/m1/s1
InChIKeyIXVAVGNSYYZTEW-OIBXWCBGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.9.2c1cc(cc(c1)Cl)c2ccc(cc2)c3cc(on3)CC(CC(=O)O)C(=O)NC(CCC(=O)O)C(=O)NC(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)=O)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)=O)Cc1onc(c1)c2ccc(cc2)c3cccc(Cl)c3
ACDLabs 12.01O=C(O)CCC(C(=O)N)NC(=O)C(CCC(O)=O)NC(=O)C(Cc1onc(c1)c2ccc(cc2)c3cccc(c3)Cl)CC(O)=O
OpenEye OEToolkits 1.9.2c1cc(cc(c1)Cl)c2ccc(cc2)c3cc(on3)C[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N
FormulaC30 H31 Cl N4 O10
Name(R)-4-(((S)-1-(((S)-1-amino-4-carboxy-1-oxobutan-2-yl)amino)-4-carboxy-1-oxobutan-2-yl)amino)-3-((3-(3'-chloro-[1,1'-biphenyl]-4-yl)isoxazol-5-yl)methyl)-4-oxobutanoate
ChEMBLCHEMBL4099825
DrugBank
ZINCZINC000584905129
PDB chain5cxa 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

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PDB5cxa Zinc-Metalloproteinase Inhibitors: Evaluation of the Complex Role Played by the Zinc-Binding Group on Potency and Selectivity.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		G178 G179 L181 T215 H218 E219 H222 H228 K233 V235 P238 T239 Y240 F248
Binding residue
(residue number reindexed from 1)		G74 G75 L77 T111 H114 E115 H118 H124 K129 V131 P134 T135 Y136 F144
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=8.05,Kd=9nM
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:5cxa, PDBe:5cxa, PDBj:5cxa
PDBsum5cxa
PubMed27996256
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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