Structure of PDB 2d22 Chain B

Receptor sequence
>2d22B (length=427) Species: 1921 (Streptomyces olivaceoviridis) [Search protein sequence]
AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKID
ATEPQRGQFNFSAGDRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGST
LRQAMIDHINGVMGHYKGKIAQWDVVSHAFSDDGSGGRRDSNLQRTGNDW
IEVAFRTARAADPAAKLCYNDYNIENWTWAKTQGVYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGASSSTYAAV
TNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL
NGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQWTYTDAGELR
VYGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVGVQSGLCLDA
VGGGTANGTLIQLYSCSNGSNQRWTRT
3D structure
PDB2d22 Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86
ChainB
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H628 N670 H707 E736 D738
Catalytic site (residue number reindexed from 1) H128 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 XYS B K548 H581 H628 Q705 E736 W766 W774 K48 H81 H128 Q205 E236 W266 W274
BS02 XYS B E544 N545 K548 Q588 E44 N45 K48 Q88
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
View graph for
Biological Process
External links
PDB RCSB:2d22, PDBe:2d22, PDBj:2d22
PDBsum2d22
PubMed19279191
UniProtQ7SI98

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