Structure of PDB 1dy4 Chain A

Receptor sequence

>1dy4A (length=434) Species: 334564 (Trichoderma reesei QM9414)

ESACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG

3D structure

• PDB: 1dy4 Structural Basis for Enantiomer Binding and Separation of a Common Beta-Blocker: Crystal Structure of Cellobiohydrolase Cel7A with Bound (S)-Propranolol at 1.9 A Resolution
• Chain: A
• Resolution: 1.9 Å

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	SNP	A	Y145 Q175 E212 E217 T246 D369 Y371 W376	Y145 Q175 E212 E217 T246 D369 Y371 W376	MOAD: Ki=44uM PDBbind-CN: -logKd/Ki=4.36,Ki=44uM
BS02	CO	A	E295 E325	E295 E325
BS03	CO	A	H206 E239	H206 E239

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1dy4, PDBe:1dy4, PDBj:1dy4
• PDBsum: 1dy4
• PubMed: 11114249
• UniProt: P62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)