Structure of PDB 3og2 Chain A Binding Site BS04

Receptor Information
>3og2 Chain A (length=986) Species: 51453 (Trichoderma reesei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKGPLQNIVTWDEHSLFVHGERVVIFSGEVHPFRLPVPSLYLDVFHKIKA
LGFNTVSFYVDWALLEGKPGRFRADGIFSLEPFFEAATKAGIYLLARPGP
YINAEVSGGGFPGWLQRVKGKLRTDAPDYLHATDNYVAHIASIIAKAQIT
NGGPVILYQPENEYSGAAEGVLFPNKPYMQYVIDQARNAGIIVPLINNDA
FPGGTGAPGTGLGSVDIYGHDGYPLGFDCAHPSAWPDNGLPTTWRQDHLN
ISPSTPFSLVEFQGGAFDPFGGWGFEQCSALVNHEFERVFYKNNMAAGVT
IFNIYMTFGGTNWGNLGHPGGYTSYDYGASIREDRRIDREKYSELKLQGQ
FLKVSPGYITATPENATQGVYSDSQNIVITPLLAKESGDFFVVRHANYSS
TDTASYTVKLPTSAGDLTIPQLGGSLTLTGRDSKIHVTDYPVGKFTLLYS
TAEIFTWNEFAEKTVLVLYGGAQELHEFAVKNPFGSSKTAKAKKIEGSNV
TIHTTSNLTVVLQWTASSARQVVQLGSLVIYMVDRNSAYNYWVPTLPGSG
KQSAYGSSLMNPDSVIINGGYLIRSVAIKGNALSVQADFNVTTPLEIIGI
PKGISKLAVNGKELGYSVSELGDWIAHPAIEIPHVQVPELTKLKWYKVDS
LPEIRSNYDDSRWPLANLRTSNNTYAPLKTPVSLYGSDYGFHAGTLLFRG
RFTARTARQQLFLSTQGGSAFASSVWLNDRFIGSFTGFDAASAANSSYTL
DRLVRGRRYILTVVVDSTGLDENWTTGDDSMKAPRGILDYALTSSSGANV
SISWKLTGNLGGEDYRDVFRGPLNEGGLFFERQGFHLPSPPLSDFTHGPS
SSSSSSSPLDGIAHAGIAFYAAKLPLHLPAQEYDIPLSFVFDNATAAAPY
RALLYVNGFQYGKYVSNIGPQTEFPVPEGILDYNGDNWIGVALWALESRG
AKVPGLALKSKSPILTGRERVEVVKGPHFKKRHGAY
Ligand information
Ligand IDBMA
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-RWOPYEJCSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O
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
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
Namebeta-D-mannopyranose;
beta-D-mannose;
D-mannose;
mannose
ChEMBL
DrugBank
ZINCZINC000003830679
PDB chain3og2 Chain C Residue 3 [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]
PDB3og2 Crystal structures of Trichoderma reesei beta-galactosidase reveal conformational changes in the active site
Resolution1.2 Å
Binding residue
(original residue number in PDB)		F775 D776
Binding residue
(residue number reindexed from 1)		F738 D739
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.23: beta-galactosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005773 vacuole

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3og2, PDBe:3og2, PDBj:3og2
PDBsum3og2
PubMed21130883
UniProtQ70SY0

[Back to BioLiP]