Structure of PDB 6grn Chain A

Receptor sequence
>6grnA (length=434) Species: 51453 (Trichoderma reesei) [Search protein sequence]
PSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG
3D structure
PDB6grn Enantioselective Binding of Propranolol and Analogues Thereof to Cellobiohydrolase Cel7A.
ChainA
Resolution1.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E212 D214 E217 H228
Catalytic site (residue number reindexed from 1) E212 D214 E217 H228
Enzyme Commision number 3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
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 CO A E295 E325 E295 E325
BS02 CO A H206 E239 H206 E239
BS03 F9B A A143 Y145 D173 Q175 E212 E217 T246 W367 D369 W376 A143 Y145 D173 Q175 E212 E217 T246 W367 D369 W376
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6grn, PDBe:6grn, PDBj:6grn
PDBsum6grn
PubMed30255965
UniProtP62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)

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