Structure of PDB 3emy Chain A

Receptor sequence
>3emyA (length=329) Species: 51453 (Trichoderma reesei) [Search protein sequence]
QTGSAPNHPSDSADSEYITSVSIGTPAQVLPLDFDTGSSDLWVFSSETPK
SSATGHAIYTPSKSSTSKKVSGASWSISYGDGSSSSGDVYTDKVTIGGFS
VNTQGVESATRVSTEFVQDTVISGLVGLAFDSGNQVRPHPQKTWFSNAAS
SLAEPLFTADLRHGQNGSYNFGYIDTSVAKGPVAYTPVDNSQGFWEFTAS
GYSVGGGKLNRNSIDGIADTGTTLLLLDDNVVDAYYANVQSAQYDNQQEG
VVFDCDEDLPSFSFGVGSSTITIPGDLLNLTPLEEGSSTCFGGLQSSSGI
GINIFGDVALKAALVVFDLGNERLGWAQK
3D structure
PDB3emy Statistical coupling analysis of aspartic proteinases based on crystal structures of the Trichoderma reesei enzyme and its complex with pepstatin A.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D32 S35 D37 W39 Y75 D215 T218
Catalytic site (residue number reindexed from 1) D35 S38 D40 W42 Y79 D219 T222
Enzyme Commision number ?
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 peptide A D32 G34 S74 Y75 G76 D77 F189 D215 G217 T218 T219 D35 G37 S78 Y79 G80 D81 F194 D219 G221 T222 T223
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3emy, PDBe:3emy, PDBj:3emy
PDBsum3emy
PubMed18675276
UniProtQ2WBH2

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