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Receptor Information

>3prs Chain A (length=330) Species: 5116 (Cryphonectria parasitica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVDGQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLT
VTGQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKA
SLDSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTST
GYAVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGG
YVFPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGI
GINIFGDVALKAAFVVFNGATTPTLGFASK

Ligand ID

RIT

InChI

InChI=1S/C37H48N6O5S2/c1-24(2)33(42-36(46)43(5)20-29-22-49-35(40-29)25(3)4)34(45)39-28(16-26-12-8-6-9-13-26)18-32(44)31(17-27-14-10-7-11-15-27)41-37(47)48-21-30-19-38-23-50-30/h6-15,19,22-25,28,31-33,44H,16-18,20-21H2,1-5H3,(H,39,45)(H,41,47)(H,42,46)/t28-,31-,32-,33-/m0/s1

InChIKey

NCDNCNXCDXHOMX-XGKFQTDJSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.7.0	CC(C)c1nc(cs1)CN(C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](Cc2ccccc2)C[C@@H]([C@H](Cc3ccccc3)NC(=O)OCc4cncs4)O
OpenEye OEToolkits 1.7.0	CC(C)c1nc(cs1)CN(C)C(=O)NC(C(C)C)C(=O)NC(Cc2ccccc2)CC(C(Cc3ccccc3)NC(=O)OCc4cncs4)O
CACTVS 3.370	CC(C)[CH](NC(=O)N(C)Cc1csc(n1)C(C)C)C(=O)N[CH](C[CH](O)[CH](Cc2ccccc2)NC(=O)OCc3scnc3)Cc4ccccc4
CACTVS 3.370	CC(C)[C@H](NC(=O)N(C)Cc1csc(n1)C(C)C)C(=O)N[C@H](C[C@H](O)[C@H](Cc2ccccc2)NC(=O)OCc3scnc3)Cc4ccccc4
ACDLabs 12.01	O=C(OCc1scnc1)NC(Cc2ccccc2)C(O)CC(NC(=O)C(NC(=O)N(Cc3nc(sc3)C(C)C)C)C(C)C)Cc4ccccc4

Formula

C37 H48 N6 O5 S2

Name

RITONAVIR;
A-84538

PDB chain

3prs Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3prs Experimental and computational active site mapping as a starting point to fragment-based lead discovery.
Resolution	1.38 Å
Binding residue (original residue number in PDB)	D15 D33 D35 G37 S78 Y79 G80 D81 D119 F194 D219 G221 T222 T223 Y226 I304
Binding residue (residue number reindexed from 1)	D15 D33 D35 G37 S78 Y79 G80 D81 D119 F194 D219 G221 T222 T223 Y226 I304
Annotation score	1
Binding affinity	PDBbind-CN: -logKd/Ki=7.82,Ki=15nM

Catalytic site (original residue number in PDB)	D35 S38 D40 W42 Y79 D219 T222
Catalytic site (residue number reindexed from 1)	D35 S38 D40 W42 Y79 D219 T222
Enzyme Commision number	3.4.23.22: endothiapepsin.

	Molecular Function
GO:0004190	aspartic-type endopeptidase activity

	Biological Process
GO:0006508	proteolysis

PDB	RCSB:3prs, PDBe:3prs, PDBj:3prs
PDBsum	3prs
PubMed	22213702
UniProt	P11838\|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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Structure of PDB 3prs Chain A Binding Site BS01