Structure of PDB 1gvw Chain A Binding Site BS01

Receptor Information
>1gvw 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 information
Ligand ID0EM
InChIInChI=1S/C32H51N6O7P/c1-8-22(4)17-34-27(39)19-46(43,44)28(14-21(2)3)38-30(41)26(16-24-18-33-20-35-24)36-29(40)25(15-23-12-10-9-11-13-23)37-31(42)45-32(5,6)7/h9-13,18,20-22,25-26,28H,8,14-17,19H2,1-7H3,(H,33,35)(H,34,39)(H,36,40)(H,37,42)(H,38,41)(H,43,44)/p+1/t22-,25-,26-,28+/m0/s1
InChIKeyZQDBBPUTYSTPQE-DYYCDWSUSA-O
SMILES
SoftwareSMILES
CACTVS 3.341CC[CH](C)CNC(=O)C[P](O)(=O)[CH](CC(C)C)NC(=O)[CH](Cc1c[nH]c[nH+]1)NC(=O)[CH](Cc2ccccc2)NC(=O)OC(C)(C)C
CACTVS 3.341CC[C@H](C)CNC(=O)C[P@](O)(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1c[nH]c[nH+]1)NC(=O)[C@H](Cc2ccccc2)NC(=O)OC(C)(C)C
ACDLabs 10.04O=C(NCC(C)CC)CP(=O)(O)C(NC(=O)C(NC(=O)C(NC(=O)OC(C)(C)C)Cc1ccccc1)Cc2cnc[nH+]2)CC(C)C
FormulaC32 H52 N6 O7 P
NameN-(tert-butoxycarbonyl)-L-phenylalanyl-N-{(1S)-1-[(R)-hydroxy(2-{[(2S)-2-methylbutyl]amino}-2-oxoethyl)phosphoryl]-3-methylbutyl}-3-(1H-imidazol-3-ium-4-yl)-L-alaninamide;
PD-130,328
ChEMBL
DrugBank
ZINC
PDB chain1gvw Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1gvw Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism
Resolution1.0 Å
Binding residue
(original residue number in PDB)		D15 D35 Y79 G80 D81 F194 D219 G221 T222 T223 F280 I304
Binding residue
(residue number reindexed from 1)		D15 D35 Y77 G78 D79 F192 D217 G219 T220 T221 F278 I302
Annotation score1
Binding affinityMOAD: Ki=110nM
PDBbind-CN: -logKd/Ki=6.96,Ki=110nM
Enzymatic activity
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.
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1gvw, PDBe:1gvw, PDBj:1gvw
PDBsum1gvw
PubMed12083527
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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