Structure of PDB 4yzt Chain A

Receptor sequence

>4yztA (length=512) Species: 1402 (Bacillus licheniformis)

ITPADLLENMSPGWNLGNTLDAVPTEGSWNNPPVREHTFDDIRDAGFKSV
RIPVTWDSHIGSAPEYPIDTDWMNRVEEVTDWALEREFYVVLNIHHDSWL
WISRMGNSQQETLDKLGKVWKQIAERFKNKSERLLFEIVNEPTGMSAYQM
NLLNREMLNIIRSTGGKNGQRLVIVGGLEDNKDELLHSFEPPDDDRIVLT
YHYYSPWDYVSNWWGRTTWGSAAEISEMEEDIKPVYEKFVREGYPVIIGE
YGTLGANEKHSKWLYHDTFVRLAHKYQMVPMWWDNGNDQFDRAERQWRDP
VVKEIVIQAGRGVPNAIIKPADLFIKKGQSISDQTVDIQLNGNVLTGIYQ
KSEPLKEGSDYTVDNAGKTVSIKASCLAKLLGQPGVKAQLTFTFHKGASQ
VMDIILYDDPKLEKSEFTISQSAISGDLKIPASLNGTKLATVKGVVDSTG
RPVLEEVWSWTPYLNYDEDFYEKDGDLYLKERVLKYLKSDSTFTFELWPK
GVEAVVKVKITP

3D structure

• PDB: 4yzt Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism.
• Chain: A
• Resolution: 1.665 Å

Enzymatic activity

• Enzyme Commision number: 3.2.1.4: cellulase.

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	H113 N158 E159 E268 W301	H95 N140 E141 E250 W283
BS02	BGC	A	N36 W47 N303	N18 W29 N285
BS03	BGC	A	N36 W47 N48	N18 W29 N30

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0008422 beta-glucosidase activity
• GO:0008810 cellulase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0000272 polysaccharide catabolic process
• GO:0005975 carbohydrate metabolic process
• GO:0009251 glucan catabolic process
• GO:0030245 cellulose catabolic process

Cellular Component

• GO:0005576 extracellular region
• GO:0009986 cell surface

External links

• PDB: RCSB:4yzt, PDBe:4yzt, PDBj:4yzt
• PDBsum: 4yzt
• PubMed: 27032335
• UniProt: Q65JI7