Structure of PDB 1r87 Chain A Binding Site BS07

Receptor Information
>1r87 Chain A (length=371) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPHISALNAPQLDQRYKNEFTIGAAVEPYQLQNEKDVQMLKRHFNSIVAE
NVMKPISIQPEEGKFNFEQADRIVKFAKANGMDIRFHTLVWHSQVPQWFF
LDKEGKPMVNETDPVKREQNKQLLLKRLETHIKTIVERYKDDIKYWDVVN
EVVGDDGKLRNSPWYQIAGIDYIKVAFQAARKYGGDNIKLYMNDYNTEVE
PKRTALYNLVKQLKEEGVPIDGIGHQSHIQIGWPSEAEIEKTINMFAALG
LDNQITELDVSMYGWPPRAYPTYDAIPKQKFLDQAARYDRLFKLYEKLSD
KISNVTFWGIADNHTWLDSRADVYYDANGNVVVDPNAPYAKVEKGKGKDA
PFVFGPDYKVKPAYWAIIDHK
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1r87 Chain A Residue 907 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1r87 Mapping glycoside hydrolase substrate subsites by isothermal titration calorimetry.
Resolution1.67 Å
Binding residue
(original residue number in PDB)		D297 A374 D377 K379
Binding residue
(residue number reindexed from 1)		D289 A366 D369 K371
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E159 N201 H236 E265 D267
Catalytic site (residue number reindexed from 1) E151 N193 H228 E257 D259
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
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:1r87, PDBe:1r87, PDBj:1r87
PDBsum1r87
PubMed15277671
UniProtP40943|XYN1_GEOSE Endo-1,4-beta-xylanase

[Back to BioLiP]