Structure of PDB 1q2e Chain A

Receptor sequence
>1q2eA (length=426) Species: 51453 (Trichoderma reesei) [Search protein sequence]
QSACTLQSETHPPLTWQKCSSGGTCTQQTGSVVIDANWRWTHATNSSTNC
YDGNTWSSTLCPDNETCAKNCCLDGAAYASTYGVTTSGNSLSIDFVTQSA
QKNVGARLYLMASDTTYQEFTLLGNEFSFDVDVSQLPCGLNGALYFVSMD
ADGGVSKYPTNTAGAKYGTGYCDSQCPRDLKFINGQANVEGWEPSSNNAN
TGIGGHGSCCSEMDIWEANSISEALTPHPCTTVGQEICEGDGCGGGTCDP
DGCDWNPYRLGNTSFYGPGSSFTLDTTKKLTVVTQFETSGAINRYYVQNG
VTFQQPNAELGSYSGNELNDDYCTAEEAEFGGSSFSDKGGLTQFKKATSG
GMVLVMSLWDDYYANMLWLDSTYPTNETSSTPGAVRGSCSTSSGVPAQVE
SQSPNAKVTFSNIKFGPIGSTGNPSG
3D structure
PDB1q2e Engineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7D
ChainA
Resolution1.75 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 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 SGC A F338 Y381 R394 F330 Y373 R386
BS02 GLC A E217 H228 D259 W376 E217 H228 D251 W368
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
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Biological Process
External links
PDB RCSB:1q2e, PDBe:1q2e, PDBj:1q2e
PDBsum1q2e
PubMed14568538
UniProtP62694|GUX1_HYPJE Exoglucanase 1 (Gene Name=cbh1)

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