Structure of PDB 4v0z Chain A

Receptor sequence

>4v0zA (length=434) Species: 334564 (Trichoderma reesei QM9414)

ESACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIGFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQDGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG

3D structure

• PDB: 4v0z Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non-productive binding: insights from crystal structures and MD simulation.
• Chain: A
• Resolution: 1.7 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	BGC	A	R251 D259 Y381 R394	R251 D259 Y381 R394
BS02	BGC	A	Q175 E217 H228 R251 D259 W376	Q175 E217 H228 R251 D259 W376
BS03	CO	A	E295 E325	E295 E325
BS04	CO	A	H206 E239	H206 E239
BS05	OPO	A	Y381 P382 R394	Y381 P382 R394

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:4v0z, PDBe:4v0z, PDBj:4v0z
• PDBsum: 4v0z
• PubMed: 35997626
• UniProt: P62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)