Structure of PDB 1v0l Chain A

Receptor sequence
>1v0lA (length=302) Species: 1916 (Streptomyces lividans) [Search protein sequence]
ESTLGAAAAQSGRYFGTAIASGRLSDSTYTSIAGREFNMVTAENEMKIDA
TEPQRGQFNFSSADRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGSAL
RQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARRDSNLQRSGNDWI
EVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPIDC
VGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVT
NDCLAVSRCLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDALN
GG
3D structure
PDB1v0l Atomic Resolution Analyses of the Binding of Xylobiose-Derived Deoxynojirimycin and Isofagomine to Xylanase Xyn10A
ChainA
Resolution0.98 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) E127 N169 H206 E235 D237
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 XIF A K48 H81 W85 E128 Q205 E236 W266 W274 K47 H80 W84 E127 Q204 E235 W265 W273 PDBbind-CN: -logKd/Ki=7.55,Ki=0.028uM
BS02 XYP A E44 N45 K48 Q88 E43 N44 K47 Q87 PDBbind-CN: -logKd/Ki=7.55,Ki=0.028uM
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:1v0l, PDBe:1v0l, PDBj:1v0l
PDBsum1v0l
PubMed15306887
UniProtP26514|XYNA_STRLI Endo-1,4-beta-xylanase A (Gene Name=xlnA)

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