Structure of PDB 1ogo Chain X Binding Site BS02

Receptor Information
>1ogo Chain X (length=572) Species: 28574 (Talaromyces minioluteus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTANTHCGADFCTWWHDSGEINTQTPVQPGNVRQSHKYSVQVSLAGTNNF
HDSFVYESIPRNGNGRIYAPTDPPNSNTLDSSVDDGISIEPSIGLNMAWS
QFEYSHDVDVKILATDGSSLGSPSDVVIRPVSISYAISQSDDGGIVIRVP
ADANGRKFSVEFKTDLYTFLSDGNEYVTSGGSVVGVEPTNALVIFASPFL
PSGMIPHMTPDNTQTMTPGPINNGDWGAKSILYFPPGVYWMNQDQSGNSG
KLGSNHIRLNSNTYWVYLAPGAYVKGAIEYFTKQNFYATGHGILSGENYV
YQANAGDNYIAVKSDSTSLRMWWHNNLGGGQTWYCVGPTINAPPFNTMDF
NGNSGISSQISDYKQVGAFFFQTDGPEIYPNSVVHDVFWHVNDDAIKIYY
SGASVSRATIWKCHNDPIIQMGWTSRDISGVTIDTLNVIHTRYIKSETVV
PSAIIGASPFYASGMSPDSRKSISMTVSNVVCEGLCPSLFRITPLQNYKN
FVVKNVAFPDGLQTNSIGTGESIIPAASGLTMGLAISAWTIGGQKVTMEN
FQANSLGQFNIDGSYWGEWQIS
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain1ogo Chain A Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ogo Dextranase from Penicillium Minioluteum. Reaction Course, Crystal Structure, and Product Complex
Resolution1.65 Å
Binding residue
(original residue number in PDB)		K315 Q374 D395 D418
Binding residue
(residue number reindexed from 1)		K313 Q372 D393 D416
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D376 D395
Catalytic site (residue number reindexed from 1) D374 D393
Enzyme Commision number 3.2.1.11: dextranase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033904 dextranase activity
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:1ogo, PDBe:1ogo, PDBj:1ogo
PDBsum1ogo
PubMed12962629
UniProtP48845|DEXT_TALMI Dextranase (Gene Name=DEX)

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