Structure of PDB 2dck Chain A

Receptor sequence
>2dckA (length=320) Species: 98930 (Bacillus sp. 41M-1) [Search protein sequence]
AITSNEIGTHDGYDYEFWKDSGGSGSMTLNSGGTFSAQWSNVNNILFRKG
KKFDETQTHQQIGNMSINYGATYNPNGNSYLTVYGWTVDPLVEFYIVDSW
GTWRPPGGTPKGTINVDGGTYQIYETTRYNQPSIKGTATFQQYWSVRTSK
RTSGTISVSEHFRAWESLGMNMGNMYEVALTVEGYQSSGSANVYSNTLTI
GATRVEAESMTKGGPYTSNITSPFNGVALYANGDNVSFNHSFTKANSSFS
LRGASNNSNMARVDLRIGGQNRGTFYFGDQYPAVYTINNINHGIGNQLVE
LIVTADDGTWDAYLDYLEIR
3D structure
PDB2dck A two-domain structure of alkaliphilic XynJ from Bacillus sp. 41M-1
ChainA
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) N44 Y84 E93 Y95 E183
Catalytic site (residue number reindexed from 1) N44 Y84 E93 Y95 E183
Enzyme Commision number 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 A E213 E215 N232 D322 E206 E208 N225 D315
BS02 CA A Y237 D313 W317 D318 Y230 D306 W310 D311
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0030246 carbohydrate binding
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2dck, PDBe:2dck, PDBj:2dck
PDBsum2dck
PubMed
UniProtQ9RC94

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