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Receptor Information

>1gvt Chain A (length=328) Species: 5116 (Cryphonectria parasitica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVT
GQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASL
DSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY
AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYV
FPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGI
NIFGDVALKAAFVVFNGATTPTLGFASK

Ligand ID

2ZS

InChI

InChI=1S/C31H48N4O7S/c1-21(2)42-30(39)27(36)24(18-22-10-6-4-7-11-22)32-29(38)26(20-43-3)33-28(37)25(19-23-12-8-5-9-13-23)34-31(40)35-14-16-41-17-15-35/h5,8-9,12-13,21-22,24-27,36H,4,6-7,10-11,14-20H2,1-3H3,(H,32,38)(H,33,37)(H,34,40)/t24-,25-,26-,27+/m0/s1

InChIKey

UZQBKCWYZBHBOW-YIPNQBBMSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	CC(C)OC(=O)[C@@H]([C@H](CC1CCCCC1)NC(=O)[C@H](CSC)NC(=O)[C@H](Cc2ccccc2)NC(=O)N3CCOCC3)O
CACTVS 3.341	CSC[CH](NC(=O)[CH](Cc1ccccc1)NC(=O)N2CCOCC2)C(=O)N[CH](CC3CCCCC3)[CH](O)C(=O)OC(C)C
ACDLabs 10.04	O=C(NC(C(=O)NC(C(=O)NC(C(O)C(=O)OC(C)C)CC1CCCCC1)CSC)Cc2ccccc2)N3CCOCC3
CACTVS 3.341	CSC[C@H](NC(=O)[C@H](Cc1ccccc1)NC(=O)N2CCOCC2)C(=O)N[C@@H](CC3CCCCC3)[C@@H](O)C(=O)OC(C)C
OpenEye OEToolkits 1.5.0	CC(C)OC(=O)C(C(CC1CCCCC1)NC(=O)C(CSC)NC(=O)C(Cc2ccccc2)NC(=O)N3CCOCC3)O

Formula

C31 H48 N4 O7 S

Name

N-(morpholin-4-ylcarbonyl)-L-phenylalanyl-N-[(1R,2S)-1-(cyclohexylmethyl)-2-hydroxy-3-(1-methylethoxy)-3-oxopropyl]-S-methyl-L-cysteinamide;
CP-80,794

PDB chain

1gvt Chain A Residue 400 [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	1gvt Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism
Resolution	0.98 Å
Binding residue (original residue number in PDB)	D15 D33 D35 Y79 G80 D81 F116 F194 D219 G221 T222 T223 F280 I300 I304
Binding residue (residue number reindexed from 1)	D15 D33 D35 Y77 G78 D79 F114 F192 D217 G219 T220 T221 F278 I298 I302
Annotation score	1

Catalytic site (original residue number in PDB)	D35 S38 D40 W42 G80 T220 T223
Catalytic site (residue number reindexed from 1)	D35 S38 D40 W42 G78 T218 T221
Enzyme Commision number	3.4.23.22: endothiapepsin.

	Molecular Function
GO:0004190	aspartic-type endopeptidase activity

	Biological Process
GO:0006508	proteolysis

PDB	RCSB:1gvt, PDBe:1gvt, PDBj:1gvt
PDBsum	1gvt
PubMed	12083527
UniProt	P11838\|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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Structure of PDB 1gvt Chain A Binding Site BS01