Structure of PDB 2vs2 Chain A

Receptor sequence
>2vs2A (length=328) Species: 5116 (Cryphonectria parasitica) [Search protein sequence]
STGSATTTPIDSLDDAYITPVQIGTPAQTLNLDFDTGSSDLWVFSSETTA
SEVQTIYTPSKSTTAKLLSGATWSISYGDGSSSSGDVYTDTVSVGGLTVT
GQAVESAKKVSSSFTEDSTIDGLLGLAFSTLNTVSPTQQKTFFDNAKASL
DSPVFTADLGYHAPGTYNFGFIDTTAYTGSITYTAVSTKQGFWEWTSTGY
AVGSGTFKSTSIDGIADTGTTLLYLPATVVSAYWAQVSGAKSSSSVGGYV
FPCSATLPSFTFGVGSARIVIPGDYIDFGPISTGSSSCFGGIQSSAGIGI
NIFGDVALKAAFVVFNGATTPTLGFASK
3D structure
PDB2vs2 The Catalytic Mechanism of an Aspartic Proteinase Explored with Neutron and X-Ray Diffraction
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 0QS A D15 A16 D33 D35 G37 S38 Y79 G80 D81 F116 L133 D219 G221 T222 T223 I300 I304 D15 A16 D33 D35 G37 S38 Y77 G78 D79 F114 L131 D217 G219 T220 T221 I298 I302
External links
PDB RCSB:2vs2, PDBe:2vs2, PDBj:2vs2
PDBsum2vs2
PubMed18479128
UniProtP11838|CARP_CRYPA Endothiapepsin (Gene Name=EAPA)

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