Structure of PDB 1axk Chain B

Receptor sequence
>1axkB (length=394) Species: 44252,224308 [Search protein sequence]
FDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHGTQWDEIDI
EFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFDWQPGYIKW
YVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGANPLYAEYDW
VKYTSNASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGNFVVGKGWTT
GSPFRTINYNAGVWAPNGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTY
KGTVKSDGGTYDIYTTTRYNAPSIDGDRTTFTQYWSVRQSKRPTGSNATI
TFSNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSSNVTVWGSVFWEPKS
YFNPSTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLGLTSSA
3D structure
PDB1axk Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 CA B D149 P348 G384 D149 P348 G384
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1axk, PDBe:1axk, PDBj:1axk
PDBsum1axk
PubMed9618460
UniProtP18429|XYNA_BACSU Endo-1,4-beta-xylanase A (Gene Name=xynA);
P23904|GUB_PAEMA Beta-glucanase

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