Structure of PDB 2c8n Chain F

Receptor sequence

>2c8nF (length=500) Species: 1515 (Acetivibrio thermocellus)

KARMTVDKDYKIAEIDKRIYGSFVEHLGRAVYDGLYQPGNSKSDEDGFRK
DVIELVKELNVPIIRYPGGNFVSNYFWEDGVGPVEDRPRRLDLAWKSIEP
NQVGINEFAKWCKKVNAEIMMAVNLGTRGISDACNLLEYCNHPGGSKYSD
MRIKHGVKEPHNIKVWCLGNAMDGPWQVGHKTMDEYGRIAEETARAMKMI
DPSIELVACGSSSKDMPTFPQWEATVLDYAYDYVDYISLHQYYGNKENDT
ADFLAKSDDLDDFIRSVIATCDYIKAKKRSKKDIYLSFDEWNVWYHSNNE
DANIMQNEPWRIAPPLLEDIYTFEDALLVGLMLITLMKHADRIKIACLAQ
LINVIAPIVTERNGGAAWRQTIFYPFMHASKYGRGIVLQPVINSPLHDTS
KHEDVTDIESVAIYNEEKEEVTIFAVNRNIHEDIVLVSDVRGMKDYRLLE
HIVLEHQDLKIRNSVNGEEVYPKNSDKSSFDDGILTSMLRRASWNVIRIG

3D structure

• PDB: 2c8n Structural Insight Into the Ligand Specificity of a Thermostable Family 51 Arabinofuranosidase, Araf51, from Clostridium Thermocellum.
• Chain: F
• Resolution: 2.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A173 E292
• Catalytic site (residue number reindexed from 1): A171 E290
• Enzyme Commision number: 3.2.1.55: non-reducing end alpha-L-arabinofuranosidase.

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	XYS	F	N72 W296	N70 W294
BS02	AHR	F	E27 G71 N72 W97 E292 Q352	E25 G69 N70 W95 E290 Q350

Gene Ontology

Molecular Function

• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0046556 alpha-L-arabinofuranosidase activity

Biological Process

• GO:0000272 polysaccharide catabolic process
• GO:0031222 arabinan catabolic process
• GO:0046373 L-arabinose metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2c8n, PDBe:2c8n, PDBj:2c8n
• PDBsum: 2c8n
• PubMed: 16336192
• UniProt: A3DIH0|IABF_ACET2 Intracellular exo-alpha-(1->5)-L-arabinofuranosidase (Gene Name=Cthe_2548)