Structure of PDB 4mwp Chain E Binding Site BS06

Receptor Information

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

ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTL
PGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAI
RSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTD
YTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGD
SLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTH
YGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTS
QEVASVKQAFDAVGVK

Ligand information

• Ligand ID: 2GC
• InChI: InChI=1S/C23H32N3O5P/c1-18(2)15-21(22(27)24-14-13-19-9-5-3-6-10-19)26-32(29,30)17-25-23(28)31-16-20-11-7-4-8-12-20/h3-12,18,21H,13-17H2,1-2H3,(H,24,27)(H,25,28)(H2,26,29,30)/t21-/m0/s1
• InChIKey: YDQXQNYYSTUPNL-NRFANRHFSA-N
• SMILES:
  OpenEye OEToolkits 1.7.6: CC(C)CC(C(=O)NCCc1ccccc1)NP(=O)(CNC(=O)OCc2ccccc2)O
  OpenEye OEToolkits 1.7.6: CC(C)C[C@@H](C(=O)NCCc1ccccc1)NP(=O)(CNC(=O)OCc2ccccc2)O
  CACTVS 3.385: CC(C)C[CH](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCCc2ccccc2
  CACTVS 3.385: CC(C)C[C@H](N[P](O)(=O)CNC(=O)OCc1ccccc1)C(=O)NCCc2ccccc2
  ACDLabs 12.01: C(OC(=O)NCP(NC(CC(C)C)C(=O)NCCc1ccccc1)(=O)O)c2ccccc2
• Formula: C23 H32 N3 O5 P
• Name: P-((((benzyloxy)carbonyl)amino)methyl)-N-((S)-4-methyl-1-oxo-1-(phenethylamino)pentan-2-yl)phosphonamidic acid;
  N~2~-[(R)-({[(benzyloxy)carbonyl]amino}methyl)(hydroxy)phosphoryl]-N-(2-phenylethyl)-L-leucinamide
• ChEMBL: CHEMBL3558970
• ZINC: ZINC000098208166
• PDB chain: 4mwp Chain E Residue 413

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4mwp 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: 1.23 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:4mwp, PDBe:4mwp, PDBj:4mwp
• PDBsum: 4mwp
• PubMed: 24623396
• UniProt: P00800|THER_BACTH Thermolysin (Gene Name=npr)