Structure of PDB 1vbr Chain B Binding Site BS02

Receptor Information
>1vbr Chain B (length=324) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VSLRELAEKLNIYIGFAAINNFWSLSDAEKYMEVARREFNILTPENQMKW
DTIHPERDRYNFTPAEKHVEFAEENDMIVHGHTLVWHNQLPGWITGREWT
KEELLNVLEDHIKTVVSHFKGRVKIWDVVNEAVSDSGTYRESVWYKTIGP
EYIEKAFRWAKEADPDAILIYNDYSIEEINAKSNFVYNMIKELKEKGVPV
DGIGFQMHIDYRGLNYDSFRRNLERFAKLGLQIYITEMDVRIPLSGSEEY
YLKKQAEVCAKIFDICLDNPAVKAIQFWGFTDKYSWVPGFFKGYGKALLF
DENYNPKPCYYAIKEVLEKKIEER
Ligand information
Ligand IDXYS
InChIInChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5+/m1/s1
InChIKeySRBFZHDQGSBBOR-LECHCGJUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C(C(C(C(O1)O)O)O)O
CACTVS 3.341O[CH]1CO[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O
CACTVS 3.341O[C@@H]1CO[C@H](O)[C@H](O)[C@H]1O
ACDLabs 10.04OC1C(O)COC(O)C1O
FormulaC5 H10 O5
Namealpha-D-xylopyranose;
alpha-D-xylose;
D-xylose;
xylose;
XYLOPYRANOSE
ChEMBL
DrugBankDB03389
ZINCZINC000001529214
PDB chain1vbr Chain D Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1vbr Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8
Resolution1.8 Å
Binding residue
(original residue number in PDB)		E561 N562 W794 W802
Binding residue
(residue number reindexed from 1)		E45 N46 W278 W286
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E647 N688 H724 E753 D755
Catalytic site (residue number reindexed from 1) E131 N172 H208 E237 D239
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:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1vbr, PDBe:1vbr, PDBj:1vbr
PDBsum1vbr
PubMed16247799
UniProtQ9WXS5

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