Structure of PDB 3voh Chain A

Receptor sequence
>3vohA (length=362) Species: 5346 (Coprinopsis cinerea) [Search protein sequence]
VPSTGNPFEGYDIYLSPYYAEEVEAAAAMIDDPVLKAKALKVKEIPTFIW
FDVVRKTPDLGRYLADATAIQQRTGRKQLVQIVVYDLPDRDCAAAASNGE
FSLADGGMEKYKDYVDRLASEIRKYPDVRIVAVIEPDSLANMVTNMNVAK
CRGAEAAYKEGVIYALRQLSALGVYSYVDAGHAGWLGWNANLAPSARLFA
QIYKDAGRSAFIRGLATNVSNYNALSATTRDPVTQGNDNYDELRFINALA
PLLRNEGWDAKFIVDQGRSGVQNIRQEWGNWCNVYGAGFGMRPTLNTPSS
AIDAIVWIKPGGEADGTSDTSAPRYDTHCGKSDSHKPAPEAGTWFQEYFV
NLVKNANPPLAA
3D structure
PDB3voh Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea - a tweezer-like motion in the structure of CcCel6C
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y158 R163 D164 S170 D210 D388
Catalytic site (residue number reindexed from 1) Y85 R90 D91 S97 D137 D315
Enzyme Commision number 3.2.1.-
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 W123 D125 S170 K382 E386 W50 D52 S97 K309 E313
BS02 BGC A Y91 W123 D125 K129 E386 G415 Y18 W50 D52 K56 E313 G342
BS03 BGC A T217 G257 W258 T144 G184 W185
BS04 BGC A N218 H255 W258 N145 H182 W185
BS05 BGC A D164 D210 W354 D91 D137 W281
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3voh, PDBe:3voh, PDBj:3voh
PDBsum3voh
PubMed22429290
UniProtB7X9Z0

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