1A81: Tandem SH2 domain of the syk kinase

Crystal structure of the tandem SH2 domain of the syk kinase bound to a dually tyrosine-phosphorylated itam. Determined by X-ray diffraction at 3.0 Å resolution. Released 21 Oct 1998.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 12
Atoms: 12,201
Mol. weight: 186.7 kDa
Released: 21 Oct 1998

Explore 1A81 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1A81 contains 57 α-helices and 91 β-strands across 12 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: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	16	1	1
α-helix	22-31	10
β-strand	38-43	6	1
β-strand	51-57	7	1
β-strand	60-68	9	1
β-strand	74-76	3	1
β-strand	82	1	1
α-helix	85-92	8
β-strand	105-106	2	1
α-helix	121-135	15
α-helix	140-160	21
α-helix	163-165	3
β-strand	169-172	4	2
α-helix	175-183	9
β-strand	192-196	5	2
β-strand	203-209	7	2
β-strand	212-218	7	2
β-strand	219-220	2	3
β-strand	226-227	2	3
β-strand	234	1	3
α-helix	237-244	8
β-strand	258	1	2

Chains B, J and L: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	175-177	3

Chain C: 11 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
β-strand	16-17	2	4
α-helix	22-32	11
β-strand	38-43	6	4
β-strand	51-57	7	4
β-strand	60-68	9	4
α-helix	69	1
β-strand	74-76	3	4
β-strand	82	1	4
α-helix	85-92	8
β-strand	105-106	2	4
α-helix	108-110	3
α-helix	121-135	15
α-helix	141-160	20
α-helix	163-165	3
β-strand	169-172	4	5
α-helix	175-183	9
β-strand	192-199	8	5
β-strand	202-209	8	5
β-strand	212-217	6	5
β-strand	219-221	3	6
β-strand	225-227	3	6
β-strand	234	1	6
α-helix	237-244	8
β-strand	258	1	5
α-helix	259-261	3

Chain D: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	170-173	4
α-helix	175-177	3
α-helix	182-184	3

Chain E: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
β-strand	16-17	2	7
α-helix	22-30	9
β-strand	38-43	6	7
β-strand	51-56	6	7
β-strand	61-69	9	7
β-strand	73-76	4	7
β-strand	82	1	7
α-helix	85-92	8
β-strand	106	1	7
α-helix	154-160	7
α-helix	163-165	3
β-strand	169-172	4	8
α-helix	175-183	9
β-strand	192-196	5	8
β-strand	202-209	8	8
β-strand	212-220	9	8
β-strand	226-227	2	8
β-strand	234	1	8
α-helix	237-244	8
β-strand	249	1	9
β-strand	251	1	9
β-strand	258	1	8

Chain F: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	171-173	3

Chain G: 8 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
β-strand	16	1	10
α-helix	22-30	9
β-strand	39-43	5	10
β-strand	51-56	6	10
β-strand	61-68	8	10
β-strand	74-76	3	10
β-strand	82	1	10
α-helix	85-94	10
β-strand	106	1	10
α-helix	154-160	7
α-helix	163-165	3
β-strand	169-172	4	11
α-helix	175-183	9
β-strand	192-196	5	11
β-strand	203-209	7	11
β-strand	212-218	7	11
β-strand	220	1	12
β-strand	226	1	12
β-strand	234	1	12
α-helix	237-244	8
β-strand	258	1	11
α-helix	259-261	3

Chain H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	171-173	3
α-helix	175-177	3

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Syk kinase	A, C, E, G, I, K	protein	254	Homo sapiens	P43405 (AlphaFold model)
T-cell surface glycoprotein CD3 epsilon chain	B, D, F, H, J, L	protein	18	Homo sapiens	P07766 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K), FASTA

>1A81_1 SYK KINASE (chains A, C, E, G, I, K)
SANHLPFFFGNITREEAEDYLVQGGMSDGLYLLRQSRNYLGGFALSVAHGRKAHHYTIER
ELNGTYAIAGGRTHASPADLCHYHSQESDGLVCLLKKPFNRPQGVQPKTGPFEDLKENLI
REYVKQTWNLQGQALEQAIISQKPQLEKLIATTAHEKMPWFHGKISREESEQIVLIGSKT
NGKFLIRARDNNGSYALCLLHEGKVLHYRIDKDKTGKLSIPEGKKFDTLWQLVEHYSYKA
DGLLRVLTVPCQKI

Sequence of entity 2 (B, D, F, H, J, L), FASTA

>1A81_2 T-CELL SURFACE GLYCOPROTEIN CD3 EPSILON CHAIN (chains B, D, F, H, J, L)
PDYEPIRKGQRDLYSGLN

Primary citation

Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. Futterer, K., Wong, J., Grucza, R.A. et al. J Mol Biol (1998) 281:523-537. DOI 10.1006/jmbi.1998.1964 · PubMed

Other PDB entries of the same protein (UniProt P43405 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4YJR 1.32 Å, SYK kinase domain in complex with inhibitor GTC000225
4YJQ 1.34 Å, SYK kinase domain in complex with inhibitor GTC000224
4FYO 1.4 Å, Crystal structure of spleen tyrosine kinase complexed with…
5LMA 1.43 Å, Human spleen tyrosine kinase kinase domain in complex with azanaphthyridine inhibitor
3BUW 1.45 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Syk
6ZCS 1.47 Å, SYK Kinase domain in complex with azabenzimidazole inhibitor 3
5TIU 1.49 Å, Crystal structure of SYK kinase domain with inhibitor
8XQ1 1.5 Å, Crystal structure of spleen tyrosine kinase(SYK) in complex with SKI-G-1673
8BI2 1.51 Å, Syk kinase domain in complex with macrocyclic inhibitor 20a
4YJT 1.52 Å, The kinase domain of human spleen tyrosine (SYK) in complex with GTC000233
1XBB 1.57 Å, Crystal structure of the syk tyrosine kinase domain with Gleevec
4RX8 1.59 Å, SYK Catalytic Domain Complexed with a Potent Triazine Inhibitor2

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