Structure of PDB 2d23 Chain B Binding Site BS03

Receptor Information

>2d23 Chain B (length=427) Species: 1921 (Streptomyces olivaceoviridis)

AESTLGAAAAQSGRYFGTAIASGKLGDSAYTTIASREFNMVTAENEMKID
ATEPQRGQFNFSAGDRVYNWAVQNGKQVRGHTLAWHSQQPGWMQSLSGST
LRQAMIDHINGVMGHYKGKIAQWDVVSHAFSDDGSGGRRDSNLQRTGNDW
IEVAFRTARAADPAAKLCYNDYNIENWTWAKTQGVYNMVRDFKQRGVPID
CVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGASSSTYAAV
TNDCLAVSRCLGITVWGVRDTDSWRSGDTPLLFNGDGSKKAAYTAVLNAL
NGGGQIKGVGSGRCLDVPNASTTDGTQVQLYDCHSATNQQWTYTDAGELR
VYGDKCLDAAGTGNGTKVQIYSCWGGDNQKWRLNSDGSIVGVQSGLCLDA
VGGGTANGTLIQLYSCSNGSNQRWTRT

Ligand information

• Ligand ID: AZI
• InChI: InChI=1S/N3/c1-3-2/q-1
• InChIKey: IVRMZWNICZWHMI-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [N-]=[N+]=[N-]
• Formula: N3
• Name: AZIDE ION
• ChEMBL: CHEMBL79455
• PDB chain: 2d23 Chain B Residue 953

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2d23 Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86
• Resolution: 1.95 Å
• Binding residue (original residue number in PDB): H628 Y672 Q705
• Binding residue (residue number reindexed from 1): H128 Y172 Q205
• Annotation score: 1

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.

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

External links

• PDB: RCSB:2d23, PDBe:2d23, PDBj:2d23
• PDBsum: 2d23
• PubMed: 19279191
• UniProt: Q7SI98