Structure of PDB 4d5v Chain A

Receptor sequence
>4d5vA (length=434) Species: 51453 (Trichoderma reesei) [Search protein sequence]
ESACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIDFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWQANSISEALTPHPCTTVGQEICEGDGCGGTYSDN
RYGGTCDPDGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAI
NRYYVQNGVTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLT
QFKKATSGGMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTS
SGVPAQVESQSPNAKVTFSNIKFGPIGSTGNPSG
3D structure
PDB4d5v Structural Insights Into the Inhibition of Cellobiohydrolase Cel7A by Xylooligosaccharides.
ChainA
Resolution1.62 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 Q217 H228
Catalytic site (residue number reindexed from 1) E212 D214 Q217 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 XYP A N37 W38 D179 N37 W38 D179
BS02 XYP A N37 W38 N103 V104 N37 W38 N103 V104
BS03 XYP A W38 Q101 W38 Q101
BS04 XLS A D173 Q175 E212 D214 Q217 W367 D173 Q175 E212 D214 Q217 W367
BS05 XYP A R107 Y145 S365 W367 R107 Y145 S365 W367
BS06 CO A E295 E325 E295 E325
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
View graph for
Biological Process
External links
PDB RCSB:4d5v, PDBe:4d5v, PDBj:4d5v
PDBsum4d5v
PubMed25765184
UniProtP62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)

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