Structure of PDB 2f8q Chain B

Receptor sequence
>2f8qB (length=353) Species: 65673 (Bacillus sp. NG-27) [Search protein sequence]
QPFAWQVASLADRYEESFDIGAAVEPHQLNGRQGKVLKHHYNSIVAENAM
KPISLQPEEGVFTWDGADAIVEFARKNNMNLRFHTLVWHNQVPDWFFLDE
EGNPMVEETNEAKRQANKELLLERLETHIKTVVERYKDDVTAWDVVNEVV
DDGTPNERGLRESVWYQITGDEYIRVAFETARKYAGEDAKLFINDYNTEV
TPKRDHLYNLVQDLLADGVPIDGVGHQAHIQIDWPTIDEIRTSMEMFAGL
GLDNQVTELDVSLYGWPPRPAFPTYDAIPQERFQAQADRYNQLFELYEEL
DADLSSVTFWGIADNHTWLDDRAREYNDGVGKDAPFVFDPNYRVKPAFWR
IID
3D structure
PDB2f8q Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditions.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E149 N195 H230 E259 D261
Catalytic site (residue number reindexed from 1) E148 N194 H229 E258 D260
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 MG B N292 R351 D354 N291 R350 D353
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
GO:0046872 metal ion binding
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:2f8q, PDBe:2f8q, PDBj:2f8q
PDBsum2f8q
PubMed16823036
UniProtO30700

[Back to BioLiP]