Structure of PDB 4uwt Chain A

Receptor sequence

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

ESACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIDFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSQMDIWEANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG

3D structure

• PDB: 4uwt Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non-productive binding: insights from crystal structures and MD simulation.
• Chain: A
• Resolution: 1.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q212 D214 E217 H228
• Catalytic site (residue number reindexed from 1): Q212 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	NPO	A	N307 G308	N307 G308
BS06	NPO	A	G339 Y381 R394	G339 Y381 R394

Gene Ontology

Molecular Function

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

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

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