Structure of PDB 1v0m Chain A

Receptor sequence
>1v0mA (length=302) Species: 1916 (Streptomyces lividans) [Search protein sequence]
AESTLGAAAAQSGRYFGTAIASGRLSDSTYTSIAGREFNMVTAENEMKID
ATEPQRGQFNFSSADRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGSA
LRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARRDSNLQRSGNDW
IEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANV
TNDCLAVSRCLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDAL
NG
3D structure
PDB1v0m Atomic Resolution Analyses of the Binding of Xylobiose-Derived Deoxynojirimycin and Isofagomine to Xylanase Xyn10A
ChainA
Resolution1.07 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E128 N170 H207 E236 D238
Catalytic site (residue number reindexed from 1) E128 N170 H207 E236 D238
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 XDN A K48 H81 W85 N127 Q205 E236 W266 W274 G302 K48 H81 W85 N127 Q205 E236 W266 W274 G302 PDBbind-CN: -logKd/Ki=5.10,Ki=8uM
BS02 XYP A E44 N45 K48 Q88 E44 N45 K48 Q88 PDBbind-CN: -logKd/Ki=5.10,Ki=8uM
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1v0m, PDBe:1v0m, PDBj:1v0m
PDBsum1v0m
PubMed15306887
UniProtP26514|XYNA_STRLI Endo-1,4-beta-xylanase A (Gene Name=xlnA)

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