2CI9: Nck1 SH2-domain

Nck1 SH2-domain in complex with a dodecaphosphopeptide from EPEC protein Tir. Determined by X-ray diffraction at 1.5 Å resolution. Released 24 Apr 2006.

Method: X-ray diffraction
Resolution: 1.5 Å
Organisms: HOMO SAPIENS, ESCHERICHIA COLI
Chains: 4
Atoms: 2,225
Mol. weight: 26.44 kDa
Released: 24 Apr 2006

Explore 2CI9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CI9 contains 6 α-helices and 20 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: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	285	1	1
α-helix	289-299	11
β-strand	304-309	6	1
β-strand	317-321	5	1
β-strand	328-332	5	1
β-strand	333-335	3	2
β-strand	338-341	4	2
β-strand	344-346	3	2
α-helix	349-358	10
β-strand	362-363	2	3
β-strand	369-370	2	3
β-strand	374-375	2	1

Chain B: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	283-285	3	4
α-helix	289-299	11
β-strand	304-309	6	4
β-strand	317-321	5	4
β-strand	328-332	5	4
β-strand	333-335	3	5
β-strand	338-341	4	5
β-strand	344-346	3	5
α-helix	349-358	10
β-strand	362-363	2	6
β-strand	369-370	2	6
β-strand	374-375	2	4

Chain L: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	473-479	7

Chain M: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	475-480	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytoplasmic protein NCK1	A, B	protein	102	HOMO SAPIENS	P16333 (AlphaFold model)
Translocated intimin receptor	L, M	protein	12	ESCHERICHIA COLI	B7UM99 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2CI9_1 CYTOPLASMIC PROTEIN NCK1 (chains A, B)
GPLGSPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLK
ETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS

Sequence of entity 2 (L, M), FASTA

>2CI9_2 TRANSLOCATED INTIMIN RECEPTOR (chains L, M)
EEHIYDEVAADP

Primary citation

The Phosphotyrosine Peptide Binding Specificity of Nck1 and Nck2 Src Homology 2 Domains. Frese, S., Schubert, W.-D., Findeis, A.C. et al. J Biol Chem (2006) 281:18236. DOI 10.1074/JBC.M512917200 · PubMed

Other PDB entries of the same protein (UniProt P16333 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5QU8 0.93 Å, Crystal Structure of symmetric swapped human Nck SH3.1 domain, 0.93A, orthorhombic form IV
5QU3 1.02 Å, Crystal Structure of domain swapped human Nck SH3.1, 1.01A, monoclinic
5QU2 1.04 Å, Crystal Structure of human Nck SH3.1 in complex with peptide PPPVPNPDY
5QU4 1.05 Å, Crystal Structure of swapped human Nck SH3.1 domain, 1.05A, orthorhombic form I
5QU1 1.08 Å, Crystal Structure of the monomeric human Nck SH3.1 domain, triclinic, 1.08A
5QU5 1.11 Å, Domain Swap in the first SH3 domain of human Nck1
5QU7 1.27 Å, Crystal Structure of swapped human Nck SH3.1 domain, 1.3A, orthorhombic form III
5QUA 1.51 Å, Crystal Structure of swapped human Nck SH3.1 domain, 1.5A, C2221
2CI8 1.8 Å, sh2 domain of human nck1 adaptor protein - uncomplexed
5QU6 1.82 Å, Crystal Structure of swapped human Nck SH3.1 domain, 1.8A, triclinic
2CUB Solution structure of the SH3 domain of the human cytoplasmic protein Nck1
2JS0 Solution structure of second SH3 domain of adaptor Nck

Browse structure collections

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