Structure of PDB 7cpl Chain A Binding Site BS01

Receptor Information

>7cpl Chain A (length=358) Species: 502601 (Bacillus sp. TAR1)

DQPFAWQVASLSERYQEQFDIGAAVEPYQLEGRQAQILKHHYNSLVAENA
MKPESLQPREGEWNWEGADKIVEFARKHNMELRFHTLVWHEQVPEWFFID
EDGNRMVDETDPDKREANKQLLLERMENHIKTVVERYKDDVTSWDVVNEV
IDDGGGLRESEWYQITGTDYIKVAFETARKYGGEEAKLYINDYNTEVPSK
RDDLYNLVKDLLEQGVPIDGVGHQSHIQIGWPSIEDTRASFEKFTSLGLD
NQVTELDMSLYGWPPTGAYTSYDDIPAELLQAQADRYDQLFELYEELAAD
ISSVTFWGIADNHTWLDGRAREYNNGVGIDAPFVFDHNYRVKPAYWRIID
LEHHHHHH

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 7cpl Chain A Residue 408

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7cpl Insight into the mechanism of thermostabilization of GH10 xylanase from Bacillus sp. strain TAR-1 by the mutation of S92 to E.
• Resolution: 1.52 Å
• Binding residue (original residue number in PDB): D289 R348 D351
• Binding residue (residue number reindexed from 1): D288 R347 D350
• Annotation score: 4

Enzymatic activity

• 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:7cpl, PDBe:7cpl, PDBj:7cpl
• PDBsum: 7cpl
• PubMed: 33604642
• UniProt: P07528|XYNA_HALH5 Endo-1,4-beta-xylanase A (Gene Name=xynA)