Structure of PDB 2yik Chain A

Receptor sequence

>2yikA (length=493) Species: 1515 (Acetivibrio thermocellus)

YNYAKALQYSMFFYDANMCGTGVDENSLLSWRGDCHVYDARLPLDSQNTN
MSDGFISSNRSVLDPDGDGKVDVSGGFHDAGDHVKFGLPEAYAASTVGWG
YYEFKDQFRATGQAVHAEVILRYFNDYFMRCTFRDASGNVVAFCHQVGDG
DIDHAFWGAPENDTMFRRGWFITKEKPGTDIISATAASLAINYMNFKDTD
PQYAAKSLDYAKALFDFAEKNPKGVVQGEDGPKGYYGSSKWQDDYCWAAA
WLYLATQNEHYLDEAFKYYDYYAPPGWIHCWNDVWSGTACILAEINDLYD
KDSQNFEDRYKRASNKNQWEQIDFWKPIQDLLDKWSGGGITVTPGGYVFL
NQWGSARYNTAAQLIALVYDKHHGDTPSKYANWARSQMDYLLGKNPLNRC
YVVGYSSNSVKYPHHRAASGLKDANDSSPHKYVLYGALVGGPDASDQHVD
RTNDYIYNEVAIDYNAAFVGACAGLYRFFGDSSMQIDPSMPSH

3D structure

• PDB: 2yik Structure of the Catalytic Domain of the Clostridium Thermocellum Cellulase Celt
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D116 D119 Y273 E496
• Catalytic site (residue number reindexed from 1): D79 D82 Y236 E459
• 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	CA	A	N333 D337 S340 E344 H530	N296 D300 S303 E307 H493
BS02	CA	A	K277 D280 D281	K240 D243 D244
BS03	CA	A	D101 D103 D105 K107	D64 D66 D68 K70
BS04	ZN	A	C56 C72 H73 H115	C19 C35 H36 H78

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046872 metal ion binding

Biological Process

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

External links

• PDB: RCSB:2yik, PDBe:2yik, PDBj:2yik
• PDBsum: 2yik
• PubMed: 22349233
• UniProt: A3DJ82