5TQS: Phospholipase C gamma-1 C-terminal SH2 domain

Phospholipase C gamma-1 C-terminal SH2 domain bound to a phosphopeptide derived from the receptor tyrosine kinase ErbB2. Determined by X-ray diffraction at 1.88 Å resolution. Released 19 Apr 2017.

Method: X-ray diffraction
Resolution: 1.88 Å
Organisms: Bos taurus, Homo sapiens
Chains: 8
Atoms: 3,803
Mol. weight: 53.98 kDa
Released: 19 Apr 2017

Explore 5TQS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TQS contains 13 α-helices and 36 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	662-665	4
β-strand	669-670	2	1
α-helix	675-683	9
β-strand	690-695	6	1
β-strand	701-708	8	1
β-strand	711-720	10	1
β-strand	723-726	4	1
β-strand	729-731	3	1
α-helix	734-741	8
β-strand	747	1	2
β-strand	750	1	2
β-strand	754-755	2	1

Chain B: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	662-665	4
β-strand	669-670	2	3
α-helix	675-683	9
β-strand	690-695	6	3
β-strand	701-708	8	3
β-strand	711-720	10	3
β-strand	723-726	4	3
β-strand	729-731	3	3
α-helix	734-743	10
β-strand	747	1	4
β-strand	750	1	4
α-helix	751-752	2
β-strand	754-755	2	3

Chain C: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	663-667	5
β-strand	669-670	2	5
α-helix	675-683	9
β-strand	690-695	6	5
β-strand	701-708	8	5
β-strand	711-719	9	5
β-strand	724-726	3	5
β-strand	729-731	3	5
α-helix	734-743	10
β-strand	747	1	6
β-strand	750	1	6
β-strand	754-755	2	5

Chain D: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	664-667	4
β-strand	669-670	2	7
α-helix	675-684	10
β-strand	690-695	6	7
β-strand	701-708	8	7
β-strand	711-720	10	7
β-strand	723-726	4	7
β-strand	729-731	3	7
α-helix	734-743	10
β-strand	747	1	8
β-strand	750	1	8
β-strand	754-755	2	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1	A, B, C, D	protein	101	Bos taurus	P08487 (AlphaFold model)
Receptor protein-tyrosine kinase	E, F, G, H	protein	11	Homo sapiens	P04626 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5TQS_1 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (chains A, B, C, D)
GSHMHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQ
QEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEE

Sequence of entity 2 (E, F, G, H), FASTA

>5TQS_2 Receptor protein-tyrosine kinase (chains E, F, G, H)
DNLYYWDQDPP

Primary citation

Multimodal Recognition of Diverse Peptides by the C-Terminal SH2 Domain of Phospholipase C-gamma 1 Protein. McKercher, M.A., Guan, X., Tan, Z. et al. Biochemistry (2017) 56:2225-2237. DOI 10.1021/acs.biochem.7b00023 · PubMed

Other PDB entries of the same protein (UniProt P08487 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5TNW 1.4 Å, Phospholipase C gamma-1 C-terminal SH2 domain
5TQ1 1.49 Å, Phospholipase C gamma-1 C-terminal SH2 domain bound to a phosphopeptide derived from the…
5TO4 1.7 Å, Phospholipase C gamma-1 C-terminal SH2 domain, spacegroup P212121
2FCI Structural basis for the requirement of two phosphotyrosines in signaling mediated by…
2PLD Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-GAMMA1…
2PLE Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-GAMMA1…

Browse structure collections

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