PDBsum entry 2l2p

Transferase

PDB id

2l2p

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Contents

			Protein chain

					56 a.a.

PDB id:

2l2p

Links
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Name:

Transferase

Title:

Folding intermediate of the fyn sh3 a39v/n53p/v55l from nmr relaxation dispersion experiments

Structure:

Tyrosine-protein kinase fyn. Chain: a. Fragment: sh3 domain (unp residues 85-142). Synonym: proto-oncogenE C-fyn, p59-fyn. Engineered: yes. Mutation: yes

Source:

Gallus gallus. Bantam,chickens. Organism_taxid: 9031. Gene: fyn. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

10 models

Authors:

P.Neudecker,P.Robustelli,A.Cavalli,M.Vendruscolo,L.E.Kay

Key ref:

P.Neudecker et al. (2012). Structure of an intermediate state in protein folding and aggregation. Science, 336, 362-366. PubMed id: 22517863

Date:

25-Aug-10

Release date:

14-Sep-11

PROCHECK

	Headers

	References

Protein chain

Q05876 (FYN_CHICK) - Tyrosine-protein kinase Fyn from Gallus gallus

Seq: Struc:

Seq: Struc:					534 a.a. 56 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 4 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.2.7.10.2 - non-specific protein-tyrosine kinase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

L-tyrosyl-[protein]	+	ATP	=	O-phospho-L-tyrosyl-[protein]	+	ADP	+	H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

	Science 336:362-366 (2012)
PubMed id: 22517863

Structure of an intermediate state in protein folding and aggregation.
P.Neudecker, P.Robustelli, A.Cavalli, P.Walsh, P.Lundström, A.Zarrine-Afsar, S.Sharpe, M.Vendruscolo, L.E.Kay.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

23041928

E.A.Dethoff, K.Petzold, J.Chugh, A.Casiano-Negroni, and H.M.Al-Hashimi (2012).
Visualizing transient low-populated structures of RNA.

Nature, 491, 724-728.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.