Structure of PDB 5gqd Chain A

Receptor sequence
>5gqdA (length=427) Species: 1921 (Streptomyces olivaceoviridis) [Search protein sequence]
AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKID
ATEPQRGQFNFSAGDRVYNWAVQNGKQVRGHALAWHSQQPGWMQSLSGST
LRQAMIDHINGVMGHYKGKIAQWDVVSHAFSDDGSGGRRDSNLQRTGNDW
IEVAFRTARAADPAAKLCYNDYNIENWTWAKTQGVYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGASSSTYAAV
TNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL
NGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQWTYTDAGELR
VYGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVGVQSGLCLDA
VGGGTANGTLIQLYSCSNGSNQRWTRT
3D structure
PDB5gqd Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
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 A K48 H81 H128 Q205 E236 W266 W274 K48 H81 H128 Q205 E236 W266 W274
BS02 XYP A E44 N45 K48 Q88 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:5gqd, PDBe:5gqd, PDBj:5gqd
PDBsum5gqd
PubMed
UniProtQ7SI98

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