Structure of PDB 7d89 Chain A Binding Site BS02

Receptor Information

>7d89 Chain A (length=351) Species: 1409 (Bacillus sp. (in: firmicutes))

QSWRKEANDRILQHRQRELVINVAGIEVEIKQIRHEFAFGSAMNDQVLFN
QTYADFFVQHFNWAVFENEAKWYANEPERGKITYEKADAMLNFANRHQIP
VRGHALFWEVEDANPNWLKSLPNHEVYEAMKRRLEHAGNHFKGKFRHWDV
NNAMMHGSFFKDRFGKQIWKWMYEETKKIDPQALLFVNDYNVISYGEHHA
YKAHINELRQLGAPVEAIGVQGHFADRVDPVVVKERLDVLAELGLPIWVT
AYDSVHPDANRRADNLEALYRVAFSHPAVKGVLMWGFWAGAHWRGEHAAI
VNHDWSLNEAGRRYEKLLQEWTTQRVEVTCPAFHGTYEVRKMLQQQTIEL
D

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: 7d89 Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7d89 Insights into the Catalytic Mechanism of a Novel XynA and Structure-Based Engineering for Improving Bifunctional Activities.
• Resolution: 2.89384 Å
• Binding residue (original residue number in PDB): Y219 N220 V221 I222 S223 G251
• Binding residue (residue number reindexed from 1): Y190 N191 V192 I193 S194 G222
• 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

External links

• PDB: RCSB:7d89, PDBe:7d89, PDBj:7d89
• PDBsum: 7d89
• PubMed: 34156819
• UniProt: A0A4P8ESF9