Structure of PDB 1ur2 Chain A Binding Site BS05

Receptor Information
>1ur2 Chain A (length=351) Species: 39650 (Cellvibrio mixtus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TGLKSAYKDNFLIGAALNATIASGADERLNTLIAKEFNSITPENCMKWGV
LRDAQGQWNWKDADAFVAFGTKHNLHMVGHTLVWHSQIHDEVFKNADGSY
ISKAALQKKMEEHITTLAGRYKGKLAAWDVVNEAVGDDLKMRDSHWYKIM
GDDFIYNAFTLANEVDPKAHLMYNDYNIERTGKREATVEMIERLQKRGMP
IHGLGIQGHLGIDTPPIAEIEKSIIAFAKLGLRVHFTSLDVDVLPSVWEL
PVAEVSTRFEYKPERDPYTKGLPQEMQDKLAKRYEDLFKLFIKHSDKIDR
ATFWGVSDDASWLNGFPIPGRTNYPLLFDRKLQPKDAYFRLLDLKRLEHH
H
Ligand information
Ligand IDAHR
InChIInChI=1S/C5H10O5/c6-1-2-3(7)4(8)5(9)10-2/h2-9H,1H2/t2-,3-,4+,5+/m0/s1
InChIKeyHMFHBZSHGGEWLO-QMKXCQHVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C([C@H]1[C@@H]([C@H]([C@@H](O1)O)O)O)O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@@H]1O[C@@H](O)[C@H](O)[C@H]1O
ACDLabs 10.04OC1C(OC(O)C1O)CO
FormulaC5 H10 O5
Namealpha-L-arabinofuranose;
alpha-L-arabinose;
L-arabinose;
arabinose
ChEMBL
DrugBankDB03142
ZINCZINC000002569310
PDB chain1ur2 Chain C Residue 3 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ur2 The Mechanisms by which Family 10 Glycoside Hydrolases Bind Decorated Substrates
Resolution1.6 Å
Binding residue
(original residue number in PDB)		E67 N68
Binding residue
(residue number reindexed from 1)		E43 N44
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E157 N198 H233 S262 D264
Catalytic site (residue number reindexed from 1) E133 N174 H209 S238 D240
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1ur2, PDBe:1ur2, PDBj:1ur2
PDBsum1ur2
PubMed14668328
UniProtO68541

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