Brand  (β version)

PDB ID: 1AYA

Hetero Atom Contents

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

Select unit:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
PTR O-phosphotyrosine
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1AYA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE(SH2 DOMAIN)
Title : CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE PHOSPHATASE
Release Data : 1994-08-31
Compound :
mol_id molecule chains
1 PROTEIN-TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN) A,B
ec: 3.1.3.48
mol_id molecule chains
2 PEPTIDE PDGFR-1009 P,Q
Source :
mol_id organism_scientific organism_common
1 Mus musculus  (taxid:10090) House mouse
mol_id organism_scientific organism_common
2 Mus musculus  (taxid:10090) House mouse
Authors : Lee, C.-H., Kuriyan, J.
Keywords : HYDROLASE(SH2 DOMAIN)
Exp. method : X-RAY DIFFRACTION ( 2.05 Å )
Citation :

Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase.

Lee, C.H.,Kominos, D.,Jacques, S.  et al.
(1994)  Structure  2 : 423 - 438

PubMed: 7521735
DOI: 10.1016/S0969-2126(00)00044-7

Binding of a High Affinity Phosphotyrosyl Peptide to the Src Sh2 Domain: Crystal Structures of the Complexed and Peptide-Free Forms

Waksman, G.,Shoelson, S.E.,Pant, N.  et al.
(1993)  Cell(Cambridge,Mass.)  72 : 779

Structures of Sh2 and SH3 Domains

Kuriyan, J.,Cowburn, D.
(1993)  Curr.Opin.Struct.Biol.  3 : 828

Crystal Structure of the Phosphotyrosine Recognition Domain Sh2 of V-Src Complexed with Tyrosine-Phosphorylated Peptides

Waksman, G.,Kominos, D.,Robertson, S.R.  et al.
(1992)  Nature  358 : 646

Reaction

Chain : A, B
UniProt : P35235 (PTN11_MOUSE)
Reaction: EC: Evidence:
Physiological Direction:
O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphate 3.1.3.48 PROSITE-ProRule:PRU10044
-
Chain : P, Q
UniProt : P05622 (PGFRB_MOUSE)
Reaction: EC: Evidence:
Physiological Direction:
L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+) 2.7.10.1 PROSITE-ProRule:PRU10028, PubMed:15284236
-