Structure of PDB 2rfz Chain A

Receptor sequence

>2rfzA (length=430) Species: 204285 (Melanocarpus albomyces)

QRAGNETPENHPPLTWQRCTAPGNCQTVNAEVVIDANWRWLHDDNMQNCY
DGNQWTNACSTATDCAEKCMIEGAGDYLGTYGASTSGDALTLKFVTKHEY
GTNVGSRFYLMNGPDKYQMFNLMGNELAFDVDLSTVECGINSALYFVAME
EDGGMASYPSNQAGARYGTGYCDAQCARDLKFVGGKANIEGWKSSTSDPN
AGVGPYGSCCAEIDVWESNAYAFAFTPHACTTNEYHVCETTNCGGTYSED
RFAGKCDANGCDYNPYRMGNPDFYGKGKTLDTSRKFTVVSRFEENKLSQY
FIQDGRKIEIPPPTWEGMPNSSEITPELCSTMFDVFNDRNRFEEVGGFEQ
LNNALRVPMVLVMSIWDDHYANMLWLDSIYPPEKEGQPGAARGDCPTDSG
VPAEVEAQFPDAQVVWSNIRFGPIGSTYDF

3D structure

• PDB: 2rfz Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding
• Chain: A
• Resolution: 1.8 Å

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	GLC	A	R251 N259 R267 Y380 P381 R392	R251 N259 R267 Y380 P381 R392
BS02	BGC	A	E217 H228 R251 W375	E217 H228 R251 W375
BS03	BGC	A	Y145 D173 Q175 E212 E217	Y145 D173 Q175 E212 E217
BS04	GLC	A	N37 W38 R107 D179 W366	N37 W38 R107 D179 W366
BS05	BGC	A	N37 W38 N103 V104 N200	N37 W38 N103 V104 N200
BS06	BGC	A	W40 N103 N200	W40 N103 N200

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

External links

• PDB: RCSB:2rfz, PDBe:2rfz, PDBj:2rfz
• PDBsum: 2rfz
• PubMed: 18499583
• UniProt: Q8J0K6