Structure of PDB 1t0o Chain A Binding Site BS01

Receptor Information
>1t0o Chain A (length=417) Species: 51453 (Trichoderma reesei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVMPDGVTGKVPSLGWNSWNAYHCDIDESKFLSAAELIVSSGLLDAGYNY
VNIDDCWSMKDGRVDGHIAPNATRFPDGIDGLAKKVHALGLKLGIYSTAG
TATCAGYPASLGYEDVDAADFADWGVDYLKYDNCNVPSDWQDEYVACNPD
FVKTGPNGTCTTALDPTLAPPGYDWSTSKSAERFGAMRNALAKQSHEIVL
SMCIWGQADVFSWGNSTGISWRMSDDISPNWGSVTRILNLNSFKLNSVDF
WGHNDADMLEVGNGNLTAAETRTHFALWAAMKSPLLIGTDLAQLSQNNIN
LLKNKHLLAFNQDSVYGQPATPYKWGINPDWTFNVTYPAEFWAGPSSKGH
LVLMVNTLDITATKEAKWNEIPGLSAGHYEVRDVWSDKDLGCLSSYKAAV
AAHDTAVILVGKKCQRW
Ligand information
Ligand IDMAN
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-PQMKYFCFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(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
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@@H]([C@H](O1)O)O)O)O)O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-mannopyranose;
alpha-D-mannose;
D-mannose;
mannose
ChEMBLCHEMBL365590
DrugBank
ZINCZINC000003860903
PDB chain1t0o Chain C Residue 5 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1t0o Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism
Resolution1.96 Å
Binding residue
(original residue number in PDB)		S242 F243 L245 T321 P322 W331
Binding residue
(residue number reindexed from 1)		S242 F243 L245 T321 P322 W331
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D132 D226
Catalytic site (residue number reindexed from 1) D132 D226
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009311 oligosaccharide metabolic process
GO:0016139 glycoside catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1t0o, PDBe:1t0o, PDBj:1t0o
PDBsum1t0o
PubMed15136043
UniProtQ92456

[Back to BioLiP]