Structure of PDB 3vof Chain A

Receptor sequence
>3vofA (length=372) Species: 5346 (Coprinopsis cinerea) [Search protein sequence]
SVNPYIGRSPLVIKSYAEKLEETIAYFEAQGDELNAARTRTVQGIPTFAW
ISDSATIDTIQPLIADAVAHQEASGEQVLVQLVIYNLPDRACAAKASDGE
FHLDDDGANKYRAYVDRIVAELSTADADKLHFSIVLEPDSLGNMVTNMHV
PKCQGAATAYKEGIAYTIASLQKPNIDLYIDAAHGGWLGWNDNLRPSAEI
FKETLDLARQITPNATVRGLAINVSNYNPYKTRAREDYTEWNNAYDEWNY
VKTLTPHLQAVGFPAQFIVDQGRSGREGIRTEWGQWCNIRNAGFGIRPTT
DQAIVDSANVDAIVWVKPGGESDGTSDVNAVRFDENCRSPASHVPAPEAG
EWFNEFVVNLVINANPPLEPTY
3D structure
PDB3vof Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea - a tweezer-like motion in the structure of CcCel6C
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y96 R101 A102 S108 D150 D334
Catalytic site (residue number reindexed from 1) Y85 R90 A91 S97 D139 D323
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 W61 S63 Y96 S108 K328 E332 G361 W50 S52 Y85 S97 K317 E321 G350
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0030245 cellulose catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3vof, PDBe:3vof, PDBj:3vof
PDBsum3vof
PubMed22429290
UniProtB7X9Z2

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