Structure of PDB 2cc0 Chain A Binding Site BS01

Receptor Information
>2cc0 Chain A (length=192) Species: 1916 (Streptomyces lividans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AACNGYVGLTFDDGPSGSTQSLLNALRQNGLRATMFNQGQYAAQNPSLVR
AQVDAGMWVANHSYTHPHMTQLGQAQMDSEISRTQQAIAGAGGGTPKLFR
PPYGETNATLRSVEAKYGLTEVIWDVDSQDWNNASTDAIVQAVSRLGNGQ
VILMHDWPANTLAAIPRIAQTLAGKGLCSGMISPQTGRAVAP
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2cc0 Chain A Residue 200 [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]
PDB2cc0 Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell Wall Degradation Reveals a Close Similarity to Peptidoglycan Deacetylases
Resolution1.6 Å
Binding residue
(original residue number in PDB)		D13 H62 H66
Binding residue
(residue number reindexed from 1)		D13 H62 H66
Annotation score4
Enzymatic activity
Enzyme Commision number 3.1.1.72: acetylxylan esterase.
Gene Ontology
Molecular Function
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2cc0, PDBe:2cc0, PDBj:2cc0
PDBsum2cc0
PubMed16431911
UniProtQ54413

[Back to BioLiP]