Structure of PDB 1isy Chain B Binding Site BS02

Receptor Information
>1isy Chain B (length=436) Species: 1921 (Streptomyces olivaceoviridis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKID
ATEPQRGQFNFSAGDRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGST
LRQAMIDHINGVMGHYKGKIAQWDVVNEAFSDDGSGGRRDSNLQRTGNDW
IEVAFRTARAADPAAKLCYNDYNIENWTWAKTQGVYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGASSSTYAAV
TNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL
NGGSSTPPPSGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQW
TYTDAGELRVYGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVG
VQSGLCLDAVGGGTANGTLIQLYSCSNGSNQRWTRT
Ligand information
Ligand IDBGC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChIKeyWQZGKKKJIJFFOK-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain1isy Chain B Residue 971 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1isy Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
Resolution2.1 Å
Binding residue
(original residue number in PDB)
D908 G911 Q921 Y923
Binding residue
(residue number reindexed from 1)
D408 G411 Q421 Y423
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E628 N670 H707 E736 D738
Catalytic site (residue number reindexed from 1) E128 N170 H207 E236 D238
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

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Molecular Function

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Biological Process
External links
PDB RCSB:1isy, PDBe:1isy, PDBj:1isy
PDBsum1isy
PubMed11829503
UniProtQ7SI98

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