Structure of PDB 4n66 Chain E Binding Site BS06

Receptor Information

>4n66 Chain E (length=316) Species: 1427 (Bacillus thermoproteolyticus)

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK

Ligand information

• Ligand ID: 2GZ
• InChI: InChI=1S/C20H34N3O5P/c1-15(2)11-17(18(24)21-13-20(3,4)5)23-29(26,27)14-22-19(25)28-12-16-9-7-6-8-10-16/h6-10,15,17H,11-14H2,1-5H3,(H,21,24)(H,22,25)(H2,23,26,27)/t17-/m0/s1
• InChIKey: GRURGYQNFDMDDQ-KRWDZBQOSA-N
• SMILES:
  OpenEye OEToolkits 1.7.6: CC(C)CC(C(=O)NCC(C)(C)C)NP(=O)(CNC(=O)OCc1ccccc1)O
  CACTVS 3.385: CC(C)C[C@H](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCC(C)(C)C
  ACDLabs 12.01: O=C(NCC(C)(C)C)C(NP(=O)(O)CNC(=O)OCc1ccccc1)CC(C)C
  OpenEye OEToolkits 1.7.6: CC(C)C[C@@H](C(=O)NCC(C)(C)C)NP(=O)(CNC(=O)OCc1ccccc1)O
  CACTVS 3.385: CC(C)C[CH](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCC(C)(C)C
• Formula: C20 H34 N3 O5 P
• Name: P-((((benzyloxy)carbonyl)amino)methyl)-N-((S)-4-methyl-1-(neopentylamino)-1-oxopentan-2-yl)phosphonamidic acid;
  N~2~-[(S)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-N-(2,2-dimethylpropyl)-L-leucinamide
• ChEMBL: CHEMBL3559030
• ZINC: ZINC000098208171
• PDB chain: 4n66 Chain E Residue 513

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4n66 Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin Inhibitors.
• Resolution: 1.44 Å
• Binding residue (original residue number in PDB): N112 A113 F114 H142 E143 H146 Y157 E166 L202 R203 H231
• Binding residue (residue number reindexed from 1): N112 A113 F114 H142 E143 H146 Y157 E166 L202 R203 H231
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H142 E143 H146 Y157 E166 D226 H231
• Catalytic site (residue number reindexed from 1): H142 E143 H146 Y157 E166 D226 H231
• Enzyme Commision number: 3.4.24.27: thermolysin.

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:4n66, PDBe:4n66, PDBj:4n66
• PDBsum: 4n66
• PubMed: 24623396
• UniProt: P00800|THER_BACTH Thermolysin (Gene Name=npr)