Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
MN Manganese (II) ion
CYU Calyculin a
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1IT6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CALYCULIN A AND THE CATALYTIC SUBUNIT OF PROTEIN PHOSPHATASE 1
Release Data : 2002-05-22
Compound :
mol_id molecule chains
1 SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT A,B
ec: 3.1.3.16
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
Authors : Kita, A., Matsunaga, S., Takai, A., Kataiwa, H., Wakimoto, T., Fusetani, N., Isobe, M., Miki, K.
Keywords : HYDROLASE-INHIBITOR COMPLEX, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Crystal structure of the complex between calyculin A and the catalytic subunit of protein phosphatase 1.

Kita, A.,Matsunaga, S.,Takai, A.  et al.
(2002)  Structure  10 : 715 - 724

PubMed: 12015153
DOI: 10.1016/S0969-2126(02)00764-5

Chain : A, B
UniProt : P36873 (PP1G_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate 3.1.3.16 PubMed:15280359
-
H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate 3.1.3.16 PubMed:15280359
-