Structure of PDB 2wze Chain A

Receptor sequence

>2wzeA (length=513) Species: 1515 (Acetivibrio thermocellus)

MDYEVVHDTFEVNFDGWCNLGVDTYLTAVENEGNNGTRGMMVINRSSASD
GAYSEKGFYLDGGVEYKYSVFVKHNGTGTETFKLSVSYLDSETEEENKEV
IATKDVVAGEWTEISAKYKAPKTAVNITLSITTDSTVDFIFDDVTITRKG
YAANAVLKDMYANYFRVGSVLNSGTVNNSSIKALILREFNSITCENEMKP
DATLVQSGSTNTNIRVSLNRAASILNFCAQNNIAVRGHTLVWHSQTPQWF
FKDNFQDNGNWVSQSVMDQRLESYIKNMFAEIQRQYPSLNLYAYDVVNAA
VSDDANRTRYYGGAREPGYGNGRSPWVQIYGDNKFIEKAFTYARKYAPAN
CKLYYNDYNEYWDHKRDCIASICANLYNKGLLDGVGMQSHINADMNGFSG
IQNYKAALQKYINIGCDVQITELDISTENGKFSLQQQADKYKAVFQAAVD
INRTSSKGKVTAVCVWGPNDANTWLGSQNAPLLFNANNQPKPAYNAVASI
IPQSEWGDGNNPA

3D structure

• PDB: 2wze Putting an N-Terminal End to the Clostridium Thermocellum Xylanase Xyn10B Story: Crystal Structure of the Cbm22-1-Gh10 Modules Complexed with Xylohexaose.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A337 N394 H428 E460 D462
• Catalytic site (residue number reindexed from 1): A299 N356 H390 E422 D424
• Enzyme Commision number: 3.2.1.8: endo-1,4-beta-xylanase.

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	XYP	A	K237 H276 W280 N336 Q426 E460 W504 W512	K199 H238 W242 N298 Q388 E422 W466 W474
BS02	XYP	A	E233 N234 K237 Q283	E195 N196 K199 Q245
BS03	CA	A	T40 E42 T68 R69 D173	T9 E11 T37 R38 D142

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

External links

• PDB: RCSB:2wze, PDBe:2wze, PDBj:2wze
• PDBsum: 2wze
• PubMed: 20682344
• UniProt: P51584|XYNY_ACETH Endo-1,4-beta-xylanase Y (Gene Name=xynY)