Structure of PDB 4pue Chain A

Receptor sequence
>4pueA (length=371) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KPHISALNAPQLDQRYKNEFTIGAAVEPYQLQNEKDVQMLKRHFNSIVAE
NVMKPISIQPEEGKFNFEQADRIVKFAKANGMDIRFHTLVWHSQVPQWFF
LDKEGKPMVNETDPVKREQNKQLLLKRLETHIKTIVERYKDDIKYWDVVN
QVVGDDGKLRNSPWYQIAGIDYIKVAFQAARKYGGDNIKLYMNDYNTEVE
PKRTALYNLVKQLKEEGVPIDGIGHQSHIQIGWPSEAEIEKTINMFAALG
LDNQITELDVSMYGWPPRAYPTYDAIPKQKFLDQAARYDRLFKLYEKLSD
KISNVTFWGIADNHTWLDSRADVYYDANGNVVVDPNAPYAKVEKGKGKDA
PFVFGPDYKVKPAYWAIIDHK
3D structure
PDB4pue Extracellulr Xylanase from Geobacillus stearothermophilus: E159Q mutant, with xylotetraose in active site.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q159 N201 H236 E265 D267
Catalytic site (residue number reindexed from 1) Q151 N193 H228 E257 D259
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 XYP A E58 N59 K62 Q102 W316 E50 N51 K54 Q94 W308
BS02 XYP A K62 H95 Q159 Q234 E265 W324 K54 H87 Q151 Q226 E257 W316
BS03 ZN A E58 H322 E50 H314
BS04 ZN A S307 I310 S299 I302
BS05 ZN A D297 A374 D377 D289 A366 D369
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
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Cellular Component
External links
PDB RCSB:4pue, PDBe:4pue, PDBj:4pue
PDBsum4pue
PubMed
UniProtP40943|XYN1_GEOSE Endo-1,4-beta-xylanase

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