Structure of PDB 1hiz Chain A

Receptor sequence
>1hizA (length=375) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
SYAKKPHISALNAPQLDQRYKNEFTIGAAVEPYQLQNEKDVQMLKRHFNS
IVAENVMKPISIQPEEGKFNFEQADRIVKFAKANGMDIRFHTLVWHSQVP
QWFFLDKEGKPMVNETDPVKREQNKQLLLKRLETHIKTIVERYKDDIKYW
DVVNEVVGDDGKLRNSPWYQIAGIDYIKVAFQAARKYGGDNIKLYMNDYN
TEVEPKRTALYNLVKQLKEEGVPIDGIGHQSHIQIGWPSEAEIEKTINMF
AALGLDNQITELDVSMYGWPPRAYPTYDAIPKQKFLDQAARYDRLFKLYE
KLSDKISNVTFWGIADNHTWLDSRADVYYDANGNVVVDPNAPYAKVEKGK
GKDAPFVFGPDYKVKPAYWAIIDHK
3D structure
PDB1hiz Structure Determination of the Extracellular Xylanase from Geobacillus Stearothermophilus by Selenomethionyl MAD Phasing
ChainA
Resolution2.4 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) E160 N202 H237 E266 D268
Catalytic site (residue number reindexed from 1) E155 N197 H232 E261 D263
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 GLA A W100 E266 W325 W95 E261 W320
BS02 GLC A N205 W242 W274 R329 N200 W237 W269 R324
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1hiz, PDBe:1hiz, PDBj:1hiz
PDBsum1hiz
PubMed15103129
UniProtP40943|XYN1_GEOSE Endo-1,4-beta-xylanase

[Back to BioLiP]