Structure of PDB 5er2 Chain E Binding Site BS01

Receptor Information

>5er2 Chain E (length=330) Species: 5116 (Cryphonectria parasitica)

STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK

Ligand information

• Ligand ID: 0EK
• InChI: InChI=1S/C50H75N9O9/c1-33(2)30-59(48(66)57-38(23-15-16-24-51)44(61)56-42(47(64)65)27-36-21-13-8-14-22-36)31-43(60)39(25-34-17-9-6-10-18-34)54-46(63)41(28-37-29-52-32-53-37)55-45(62)40(26-35-19-11-7-12-20-35)58-49(67)68-50(3,4)5/h7-8,11-14,19-22,29,32-34,38-43,60H,6,9-10,15-18,23-28,30-31,51H2,1-5H3,(H,52,53)(H,54,63)(H,55,62)(H,56,61)(H,57,66)(H,58,67)(H,64,65)/p+2/t38-,39-,40-,41-,42-,43-/m0/s1
• InChIKey: QBCYEBFUOBJJAC-KHVQSSSXSA-P
• SMILES:
  CACTVS 3.341: CC(C)CN(C[CH](O)[CH](CC1CCCCC1)NC(=O)[CH](Cc2c[nH]c[nH+]2)NC(=O)[CH](Cc3ccccc3)NC(=O)OC(C)(C)C)C(=O)N[CH](CCCC[NH3+])C(=O)N[CH](Cc4ccccc4)C(O)=O
  CACTVS 3.341: CC(C)CN(C[C@H](O)[C@H](CC1CCCCC1)NC(=O)[C@H](Cc2c[nH]c[nH+]2)NC(=O)[C@H](Cc3ccccc3)NC(=O)OC(C)(C)C)C(=O)N[C@@H](CCCC[NH3+])C(=O)N[C@@H](Cc4ccccc4)C(O)=O
  ACDLabs 10.04: O=C(O)C(NC(=O)C(NC(=O)N(CC(C)C)CC(O)C(NC(=O)C(NC(=O)C(NC(=O)OC(C)(C)C)Cc1ccccc1)Cc2cnc[nH+]2)CC3CCCCC3)CCCC[NH3+])Cc4ccccc4
• Formula: C50 H77 N9 O9
• Name: 6-ammonio-N-{[(2R,3R)-3-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1H-imidazol-3-ium-4-yl)-L-alanyl]amino}-4-cyclohexyl-2-hydroxybutyl](2-methylpropyl)carbamoyl}-L-norleucyl-L-phenylalanine;
  CP-69,799
• PDB chain: 5er2 Chain E Residue 327

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5er2 High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D30 D32 G34 Y75 G76 D77 D114 L128 F189 I213 D215 G217 T218 T219 I297 I301
• Binding residue (residue number reindexed from 1): D33 D35 G37 Y79 G80 D81 D119 L133 F194 I217 D219 G221 T222 T223 I300 I304
• Annotation score: 1
• Binding affinity: MOAD: Ki=0.27uM
  PDBbind-CN: -logKd/Ki=6.57,Ki=0.27uM

Enzymatic activity

• Enzyme Commision number: 3.4.23.22: endothiapepsin.

Gene Ontology

Molecular Function

• GO:0004190 aspartic-type endopeptidase activity

Biological Process

• GO:0006508 proteolysis

External links

• PDB: RCSB:5er2, PDBe:5er2, PDBj:5er2
• PDBsum: 5er2
• PubMed: 2676515
• UniProt: P11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)