Structure of PDB 1e0x Chain B

Receptor sequence
>1e0xB (length=309) Species: 1916 (Streptomyces lividans) [Search protein sequence]
AESTLGAAAAQSGRYFGTAIASGRLSDSTYTSIAGREFNMVTAENEMKID
ATEPQRGQFNFSSADRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGSA
LRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARRDSNLQRSGNDW
IEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANV
TNDCLAVSRCLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDAL
NGGDSSEPP
3D structure
PDB1e0x Substrate Specificity in Glycoside Hydrolase Family 10. Structural and Kinetic Analysis of the Streptomyces Lividans Xylanase 10A
ChainB
Resolution1.65 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 X2F B P308 P309 P308 P309
BS02 X2F B K48 H81 Q205 H207 E236 W266 W274 K48 H81 Q205 H207 E236 W266 W274
BS03 XYP B E44 N45 K48 Q88 W266 W274 E44 N45 K48 Q88 W266 W274
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:1e0x, PDBe:1e0x, PDBj:1e0x
PDBsum1e0x
PubMed10930426
UniProtP26514|XYNA_STRLI Endo-1,4-beta-xylanase A (Gene Name=xlnA)

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