Structure of PDB 2fgl Chain B

Receptor sequence

>2fglB (length=354) Species: 65673 (Bacillus sp. NG-27)

VQPFAWQVASLADRYEESFDIGAAVEPHQLNGRQGKVLKHHYNSIVAENA
MKPISLQPEEGVFTWDGADAIVEFARKNNMNLRFHTLVWHNQVPDWFFLD
EEGNPMVEETNEAKRQANKELLLERLETHIKTVVERYKDDVTAWDVVNEV
VDDGTPNERGLRESVWYQITGDEYIRVAFETARKYAGEDAKLFINDYNTE
VTPKRDHLYNLVQDLLADGVPIDGVGHQAHIQIDWPTIDEIRTSMEMFAG
LGLDNQVTELDVSLYGWPPRPAFPTYDAIPQERFQAQADRYNQLFELYEE
LDADLSSVTFWGIADNHTWLDDRAREYNDGVGKDAPFVFDPNYRVKPAFW
RIID

3D structure

• PDB: 2fgl 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.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E149 N195 H230 E259 D261
• Catalytic site (residue number reindexed from 1): E149 N195 H230 E259 D261
• 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	XYS	B	K52 H85 W89 N148 Q228 E259 W319	K52 H85 W89 N148 Q228 E259 W319
BS02	XYS	B	E48 N49 K52	E48 N49 K52
BS03	XYS	B	E48 N49 H317	E48 N49 H317
BS04	MG	B	N292 R351 D354	N292 R351 D354
BS05	MG	B	S18 D302 L305	S18 D302 L305

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

External links

• PDB: RCSB:2fgl, PDBe:2fgl, PDBj:2fgl
• PDBsum: 2fgl
• PubMed: 16823036
• UniProt: O30700