Structure of PDB 1isy Chain B

Receptor sequence
>1isyB (length=436) Species: 1921 (Streptomyces olivaceoviridis) [Search protein sequence]
AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKID
ATEPQRGQFNFSAGDRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGST
LRQAMIDHINGVMGHYKGKIAQWDVVNEAFSDDGSGGRRDSNLQRTGNDW
IEVAFRTARAADPAAKLCYNDYNIENWTWAKTQGVYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGASSSTYAAV
TNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL
NGGSSTPPPSGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQW
TYTDAGELRVYGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVG
VQSGLCLDAVGGGTANGTLIQLYSCSNGSNQRWTRT
3D structure
PDB1isy Crystal structures of the sugar complexes of Streptomyces olivaceoviridis E-86 xylanase: sugar binding structure of the family 13 carbohydrate binding module.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 BGC B D825 P827 N828 Q838 Y840 H843 N847 D325 P327 N328 Q338 Y340 H343 N347
BS02 BGC B D908 G911 Q921 Y923 D408 G411 Q421 Y423
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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