Structure of PDB 2v3i Chain A

Receptor sequence

>2v3iA (length=434) Species: 51453 (Trichoderma reesei)

ESACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG

3D structure

• PDB: 2v3i A Study of the Chiral Recognition Mechanisms of Cellobiohydrolase Cel7A for Ligands Based on the Beta-Blocker Motif: Crystal Structures, Microcalorimetry and Computational Modelling of Cel7A-Inhibitor Complexes.
• Chain: A
• Resolution: 1.05 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	CO	A	E295 E325	E295 E325
BS02	CO	A	H206 E239	H206 E239
BS03	XX6	A	Y145 D173 Q175 E212 E217 R251 D259 W367 W376	Y145 D173 Q175 E212 E217 R251 D259 W367 W376

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:2v3i, PDBe:2v3i, PDBj:2v3i
• PDBsum: 2v3i
• UniProt: P62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)