4XZ0: ZAP-70-tSH2:compound-A complex

ZAP-70-tSH2:compound-A complex. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Jun 2015.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,155
Mol. weight: 30.1 kDa
Ligands: 4N5
Released: 17 Jun 2015

Explore 4XZ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4XZ0 contains 14 α-helices and 17 β-strands across 1 chain. 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: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	11	1	1
β-strand	13	1	2
α-helix	17-25	9
β-strand	33-38	6	1
β-strand	46-52	7	1
β-strand	55-63	9	1
α-helix	64	1
β-strand	69-71	3	1
β-strand	77	1	1
α-helix	80-89	10
β-strand	101	1	1
α-helix	103-105	3
α-helix	108-110	3
β-strand	111	1	2
α-helix	112	1
α-helix	114-117	4
α-helix	118-123	6
α-helix	124-131	8
α-helix	138-141	4
α-helix	147-155	9
α-helix	157-160	4
β-strand	164	1	3
α-helix	170-178	9
β-strand	187-191	5	3
β-strand	198-204	7	3
β-strand	207-213	7	3
β-strand	214-215	2	4
β-strand	221-222	2	4
β-strand	228-229	2	4
α-helix	232-239	8
β-strand	253	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tyrosine-protein kinase ZAP-70	A	protein	262	Homo sapiens	P43403 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4XZ0_1 Tyrosine-protein kinase ZAP-70 (chains A)
GPHMPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFH
HFPIERQLNGTYAIAGGKAHCGPAELCEFYSRDPDGLPCNLRKPCNRPSGLEPQPGVFDC
LRDAMVRDYVRQTWKLEGEALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKL
YSGAQTDGKFLLRPRKEQGTYALSLIYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVE
YLKLKADGLIYCLKEACPNSSA

Ligands and cofactors

ID	Name	Formula	Copies
4N5	1-(3-{5-[(3-chlorobenzyl)sulfonyl]-1H-tetrazol-1-yl}phenyl)ethanone	C16 H13 Cl N4 O3 S	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding. Visperas, P.R., Winger, J.A., Horton, T.M. et al. Biochem J (2015) 465:149-161. DOI 10.1042/BJ20140793 · PubMed

Other PDB entries of the same protein (UniProt P43403 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7SIY 1.48 Å, cCBL TKB domain in complex with pZAP70 peptide
2OQ1 1.9 Å, Tandem SH2 domains of ZAP-70 with 19-mer zeta1 peptide
2Y1N 2.0 Å, Structure of c-Cbl-ZAP-70 peptide complex
2CBL 2.1 Å, N-terminal domain of cbl in complex with its binding site on zap-70
3ZNI 2.21 Å, Structure of phosphoTyr363-Cbl-b - UbcH5B-Ub - ZAP-70 peptide complex
1U59 2.3 Å, Crystal Structure of the ZAP-70 Kinase Domain in Complex with Staurosporine
5O76 2.47 Å, Structure of phosphoY371 c-CBL in complex with ZAP70-peptide and UbV.pCBL ubiquitin…
1M61 2.5 Å, Crystal structure of the apo SH2 domains of ZAP-70
2OZO 2.6 Å, Autoinhibited intact human ZAP-70
4A4C 2.7 Å, Structure of phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex
4A4B 2.79 Å, Structure of modified phosphoTyr371-c-Cbl-UbcH5B-ZAP-70 complex
4XZ1 2.8 Å, ZAP-70-tSH2:Compound-B adduct

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