Brand  (β version)

PDB ID: 1AOU

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Ligands
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Non-standard Residues
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PTR O-phosphotyrosine
Glycosylation
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Modification
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Structure summary

Code : 1AOU   PDBj   RCSB PDB   PDBe
Header : COMPLEX (PROTO-ONCOGENE/EARLY PROTEIN)
Title : NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, 22 STRUCTURES
Release Data : 1998-01-14
Compound :
mol_id molecule chains synonym
1 FYN PROTEIN-TYROSINE KINASE F SRC HOMOLOGY 2 DOMAIN
ec: 2.7.1.112
fragment: SH2 DOMAIN
mutation: C97S, C98S, C104S
mol_id molecule chains
2 PHOSPHOTYROSYL PEPTIDE P
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
cell_line: BL21
gene: LYSS
expression_system_strain: BL21 (DE3)
expression_system_cellular_location: CYTOPLASM
expression_system_plasmid: PRK172
expression_system_gene: LYSS
mol_id organism_scientific
2 Hamster polyomavirus  (taxid:10626)
Authors : Mulhern, T.D., Shaw, G.L., Morton, C.J., Day, A.J., Campbell, I.D.
Keywords : SH2 DOMAIN, SIGNAL TRANSDUCTION, PEPTIDE COMPLEX, COMPLEX (PROTO-ONCOGENE-EARLY PROTEIN), COMPLEX (PROTO-ONCOGENE-EARLY PROTEIN) complex
Exp. method : SOLUTION NMR
Citation :

The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.

Mulhern, T.D.,Shaw, G.L.,Morton, C.J.  et al.
(1997)  Structure  5 : 1313 - 1323

PubMed: 9351806
DOI: 10.1016/S0969-2126(97)00283-9

Solution Studies of the Sh2 Domain from the Fyn Tyrosine Kinase: Secondary Structure, Backbone Dynamics and Protein Association

Pintar, A.,Hensmann, M.,Jumel, K.  et al.
(1996)  Eur.Biophys.J.  24 : 371

Reaction

Chain : F
UniProt : P06241 (FYN_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+) 2.7.10.2 PROSITE-ProRule:PRU10028, PubMed:11005864, PubMed:11162638, PubMed:12788081, PubMed:14707117, PubMed:14761972, PubMed:15536091, PubMed:16841086, PubMed:17194753, PubMed:18056706, PubMed:18258597, PubMed:19179337, PubMed:19652227, PubMed:7568038
-
Cofactor: Evidence: Note:
Mn(2+) - -
Chain : P
UniProt : P03079 (MT_POVHA)
Reaction : -