Structure of PDB 1axk Chain B Binding Site BS01
Receptor Information
>1axk Chain B (length=394) Species:
44252,224308
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FDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHGTQWDEIDI
EFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFDWQPGYIKW
YVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGANPLYAEYDW
VKYTSNASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTT
GSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTY
KGTVKSDGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATI
TFSNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSSNVTVWGSVFWEPKS
YFNPSTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLGLTSSA
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
1axk Chain B Residue 395 [
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Receptor-Ligand Complex Structure
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PDB
1axk
Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
D149 P348 G384
Binding residue
(residue number reindexed from 1)
D149 P348 G384
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
E47 D49 E51 N191 Y225 E234 Y236 E328
Catalytic site (residue number reindexed from 1)
E47 D49 E51 N191 Y225 E234 Y236 E328
Enzyme Commision number
3.2.1.73
: licheninase.
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1axk
,
PDBe:1axk
,
PDBj:1axk
PDBsum
1axk
PubMed
9618460
UniProt
P18429
|XYNA_BACSU Endo-1,4-beta-xylanase A (Gene Name=xynA);
P23904
|GUB_PAEMA Beta-glucanase
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