Structure of PDB 4gr3 Chain A Binding Site BS06

Receptor Information
>4gr3 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 IDR45
InChIInChI=1S/C29H32BrN4O10P/c30-19-6-8-21(9-7-19)45(42,43)16-18(14-20-15-24(34-44-20)17-4-2-1-3-5-17)28(40)33-23(11-13-26(37)38)29(41)32-22(27(31)39)10-12-25(35)36/h1-9,15,18,22-23H,10-14,16H2,(H2,31,39)(H,32,41)(H,33,40)(H,35,36)(H,37,38)(H,42,43)/t18-,22+,23+/m1/s1
InChIKeyRXBMEHOLQJITJI-LEOXJPRUSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(O)CCC(C(=O)N)NC(=O)C(NC(=O)C(CP(=O)(O)c1ccc(Br)cc1)Cc3onc(c2ccccc2)c3)CCC(=O)O
OpenEye OEToolkits 1.7.6c1ccc(cc1)c2cc(on2)CC(CP(=O)(c3ccc(cc3)Br)O)C(=O)NC(CCC(=O)O)C(=O)NC(CCC(=O)O)C(=O)N
CACTVS 3.370NC(=O)[CH](CCC(O)=O)NC(=O)[CH](CCC(O)=O)NC(=O)[CH](Cc1onc(c1)c2ccccc2)C[P](O)(=O)c3ccc(Br)cc3
CACTVS 3.370NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](Cc1onc(c1)c2ccccc2)C[P](O)(=O)c3ccc(Br)cc3
OpenEye OEToolkits 1.7.6c1ccc(cc1)c2cc(on2)C[C@H](CP(=O)(c3ccc(cc3)Br)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N
FormulaC29 H32 Br N4 O10 P
NameN-{(2S)-3-[(S)-(4-bromophenyl)(hydroxy)phosphoryl]-2-[(3-phenyl-1,2-oxazol-5-yl)methyl]propanoyl}-L-alpha-glutamyl-L-al pha-glutamine;
RXP470A
ChEMBLCHEMBL2316256
DrugBank
ZINCZINC000095595470
PDB chain4gr3 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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PDB4gr3 Molecular determinants of a selective matrix metalloprotease-12 inhibitor: insights from crystallography and thermodynamic studies.
Resolution1.494 Å
Binding residue
(original residue number in PDB)		H172 G179 I180 L181 A182 H183 T215 H218 E219 H222 H228 V235 F237 T239 Y240
Binding residue
(residue number reindexed from 1)		H68 G75 I76 L77 A78 H79 T111 H114 E115 H118 H124 V131 F133 T135 Y136
Annotation score1
Binding affinityMOAD: Ki=15.5nM
PDBbind-CN: -logKd/Ki=7.81,Ki=15.5nM
BindingDB: Ki=16nM
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:4gr3, PDBe:4gr3, PDBj:4gr3
PDBsum4gr3
PubMed23343195
UniProtP39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)

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