Structure of PDB 4inu Chain H Binding Site BS01

Receptor Information

>4inu Chain H (length=222) Species: 4932 (Saccharomyces cerevisiae)

TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAA
DTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIV
AGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEE
AIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQ
KSYKFPRGTTAVLKESIVNICD

Ligand information

• Ligand ID: 1G6
• InChI: InChI=1S/C37H50N8O5S/c1-25(2)19-32(35(46)41-31(17-18-51(3,49)50)20-27-9-13-29(23-38)14-10-27)42-36(47)33(21-28-11-15-30(24-39)16-12-28)43-37(48)34(44-45-40)22-26-7-5-4-6-8-26/h4-16,25,31-34H,17-24,38-39H2,1-3H3,(H,41,46)(H,42,47)(H,43,48)/t31-,32+,33-,34+/m1/s1
• InChIKey: QRQMUCDZCOVIHS-ITHRCTNCSA-N
• SMILES:
  ACDLabs 12.01: NCc1ccc(CC(CCS(C)(=O)=O)NC(=O)C(CC(C)C)NC(=O)C(Cc2ccc(CN)cc2)NC(=O)C(Cc2ccccc2)\N=[N+]=[N-])cc1
  OpenEye OEToolkits 2.0.7: CC(C)C[C@@H](C(=O)N[C@H](CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)[C@@H](Cc2ccc(cc2)CN)NC(=O)[C@H](Cc3ccccc3)N=[N+]=[N-]
  CACTVS 3.385: CC(C)C[CH](NC(=O)[CH](Cc1ccc(CN)cc1)NC(=O)[CH](Cc2ccccc2)N=[N+]=[N-])C(=O)N[CH](CC[S](C)(=O)=O)Cc3ccc(CN)cc3
  OpenEye OEToolkits 2.0.7: CC(C)CC(C(=O)NC(CCS(=O)(=O)C)Cc1ccc(cc1)CN)NC(=O)C(Cc2ccc(cc2)CN)NC(=O)C(Cc3ccccc3)N=[N+]=[N-]
  CACTVS 3.385: CC(C)C[C@H](NC(=O)[C@@H](Cc1ccc(CN)cc1)NC(=O)[C@H](Cc2ccccc2)N=[N+]=[N-])C(=O)N[C@H](CC[S](C)(=O)=O)Cc3ccc(CN)cc3
• Formula: C37 H50 N8 O5 S
• Name: N3Phe-Phe(4-NH2CH2)-Leu-Phe(4-NH2CH2)-methyl vinyl sulfone, bound form
• PDB chain: 4inu Chain H Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4inu Incorporation of Non-natural Amino Acids Improves Cell Permeability and Potency of Specific Inhibitors of Proteasome Trypsin-like Sites.
• Resolution: 3.1 Å
• Binding residue (original residue number in PDB): T1 S20 T21 Q22 A27 K33 G47 A49 T52 S129
• Binding residue (residue number reindexed from 1): T1 S20 T21 Q22 A27 K33 G47 A49 T52 S129
• Annotation score: 1
• Binding affinity: PDBbind-CN: -logKd/Ki=9.26,IC50=0.55nM

Enzymatic activity

• Catalytic site (original residue number in PDB): T1 D17 R19 K33 G47 S129 D166 S169
• Catalytic site (residue number reindexed from 1): T1 D17 R19 K33 G47 S129 D166 S169
• Enzyme Commision number: 3.4.25.1: proteasome endopeptidase complex.

Gene Ontology

Molecular Function

• GO:0004298 threonine-type endopeptidase activity

Biological Process

• GO:0051603 proteolysis involved in protein catabolic process

Cellular Component

• GO:0005839 proteasome core complex

External links

• PDB: RCSB:4inu, PDBe:4inu, PDBj:4inu
• PDBsum: 4inu
• PubMed: 23320547
• UniProt: P25043|PSB2_YEAST Proteasome subunit beta type-2 (Gene Name=PUP1)