Structure of PDB 6k9r Chain A Binding Site BS02

Receptor Information

>6k9r Chain A (length=189) Species: 1344414 (Trichoderma reesei RUT C-30)

TIQPGTGYNNGYFYSYWNDGHGGVTYTNGPGGQFSVNWSNSGEFVGGKGW
QPGTKNKVINFSGSYNPNGNSYLSVYGWSRNPLIEYYIVENFGTYNPSTG
ATKLGEVTSDGSVYDIYRTQRVNQPSIIGTATFYQYWSVRRNHRSSGSVN
TANHFNAWAQQGLTLGTMDYQIVAVQGYFSSGSASITVS

Ligand information

• Ligand ID: XYP
• InChI: InChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5-/m1/s1
• InChIKey: SRBFZHDQGSBBOR-KKQCNMDGSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: C1C(C(C(C(O1)O)O)O)O
  CACTVS 3.341: O[C@@H]1CO[C@@H](O)[C@H](O)[C@H]1O
  OpenEye OEToolkits 1.5.0: C1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O
  CACTVS 3.341: O[CH]1CO[CH](O)[CH](O)[CH]1O
  ACDLabs 10.04: OC1C(O)COC(O)C1O
• Formula: C5 H10 O5
• Name: beta-D-xylopyranose;
  beta-D-xylose;
  D-xylose;
  xylose
• ZINC: ZINC000001529215
• PDB chain: 6k9r Chain B Residue 2

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6k9r Studying the Role of a Single Mutation of a Family 11 Glycoside Hydrolase Using High-Resolution X-ray Crystallography.
• Resolution: 1.3 Å
• Binding residue (original residue number in PDB): W18 Y77 S127 Y171
• Binding residue (residue number reindexed from 1): W17 Y76 S126 Y170
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): E44 Y77 E86 Y88 Q177
• Catalytic site (residue number reindexed from 1): E43 Y76 E85 Y87 Q176
• Enzyme Commision number: 3.2.1.8: endo-1,4-beta-xylanase.

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0031176 endo-1,4-beta-xylanase activity

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0045493 xylan catabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:6k9r, PDBe:6k9r, PDBj:6k9r
• PDBsum: 6k9r
• PubMed: 33128114
• UniProt: P36217|XYN2_HYPJR Endo-1,4-beta-xylanase 2 (Gene Name=xyn2)