Structure of PDB 8bhh Chain B Binding Site BS01

Receptor Information
>8bhh Chain B (length=504) Species: 5507 (Fusarium oxysporum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DFAAKCAGFKTSLKLPNTKVWFTEHVPAGKNITFPDNHPTCTPKSTITDV
EICRVAMFVTTGPKSNLTLEAWLPSNWTGRFLSTGNGGMAGCIQYDDVAY
GAGFGFATVGANNGHNGTSAVSMYKNSGVVEDYVYRSVHTGTVLGKELTK
KFYGKKHTKSYYLGCSTGGRQGWKEAQSFPDDFDGIVAGAPAMRFNGLQS
RSGSFWGITGPPGAPTHLSPEEWAMVQKNVLVQCDEPLDGVADGILEDPN
LCQYRPEALVCTKNCLTGPQIETVRKVFGPLYGNNGTYIYPRIPPGADQG
FGFAIGEQPFPYSTEWFQYVIWNDTKWDPNTIGPNDYQKASEVNPFNVET
WEGDLSKFRKRGSKIIHWHGLEDGLISSDNSMEYYNHVSATMGLSNTELD
EFYRYFRVSGCGHCSGGIGANRIGNNRANLGGKEAKNNVLLALVKWVEEG
QAPETITGVRYVNGATTGKVEVERRHCRYPYRNVWDRKGNYKNPDSWKCE
LPLE
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 chain8bhh Chain G Residue 10 [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]
PDB8bhh Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		F57 E59
Binding residue
(residue number reindexed from 1)		F22 E24
Annotation score4
Enzymatic activity
Enzyme Commision number 3.1.1.-
3.1.1.73: feruloyl esterase.
Gene Ontology
Molecular Function
GO:0030600 feruloyl esterase activity
GO:0046872 metal ion binding
GO:0052689 carboxylic ester hydrolase activity
Biological Process
GO:0045493 xylan catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8bhh, PDBe:8bhh, PDBj:8bhh
PDBsum8bhh
PubMed36961270
UniProtA0A2H3G048

[Back to BioLiP]