Structure of PDB 2bvw Chain B

Receptor sequence
>2bvwB (length=360) Species: 34413 (Humicola insolens) [Search protein sequence]
GNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDR
NVTVDTLLVQTLSEIREANQAGANPQYAAQIVVYDLPDRDCAAAASNGEW
AIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKC
SGAASTYRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAK
IYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPNYDEKHYIEAFRP
LLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQ
YVDAFVWVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFI
QLLRNANPPF
3D structure
PDB2bvw Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding.
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y174 R179 D180 S186 D226 D405
Catalytic site (residue number reindexed from 1) Y84 R89 D90 S96 D136 D315
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 GLC B G273 W274 G183 W184
BS02 BGC B N234 H271 W274 W371 N144 H181 W184 W281
BS03 BGC B D226 N310 W371 D136 N220 W281
BS04 BGC B W137 D139 S186 K399 P400 E403 G432 W47 D49 S96 K309 P310 E313 G342
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:2bvw, PDBe:2bvw, PDBj:2bvw
PDBsum2bvw
PubMed10413461
UniProtQ9C1S9|GUX6_HUMIN Exoglucanase-6A (Gene Name=cel6A)

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