Structure of PDB 2rg0 Chain C

Receptor sequence
>2rg0C (length=430) Species: 204285 (Melanocarpus albomyces) [Search protein sequence]
QRAGNETPENHPPLTWQRCTAPGNCQTVNAEVVIDANWRWLHDDNMQNCY
DGNQWTNACSTATDCAEKCMIEGAGDYLGTYGASTSGDALTLKFVTKHEY
GTNVGSRFYLMNGPDKYQMFNLMGNELAFDVDLSTVECGINSALYFVAME
EDGGMASYPSNQAGARYGTGYCDAQCARDLKFVGGKANIEGWKSSTSDPN
AGVGPYGSCCAEIDVWESNAYAFAFTPHACTTNEYHVCETTNCGGTYSED
RFAGKCDANGCDYNPYRMGNPDFYGKGKTLDTSRKFTVVSRFEENKLSQY
FIQDGRKIEIPPPTWEGMPNSSEITPELCSTMFDVFNDRNRFEEVGGFEQ
LNNALRVPMVLVMSIWDDHYANMLWLDSIYPPEKEGQPGAARGDCPTDSG
VPAEVEAQFPDAQVVWSNIRFGPIGSTYDF
3D structure
PDB2rg0 Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding
ChainC
Resolution2.1 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.-
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 BGC C N259 D262 R267 Y380 R392 N259 D262 R267 Y380 R392
BS02 BGC C E217 R251 N259 W375 E217 R251 N259 W375
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
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:2rg0, PDBe:2rg0, PDBj:2rg0
PDBsum2rg0
PubMed18499583
UniProtQ8J0K6

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