6H6A: UNC119

Crystal structure of UNC119 in complex with LCK peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Sept 2018.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
6
Atoms
4,672
Mol. weight
70.25 kDa
Ligands
15P, MYR, PO4
Released
26 Sept 2018

Explore 6H6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6H6A contains 19 α-helices and 31 β-strands across 3 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 D: 7 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix62-643
α-helix79-813
β-strand87-9591
β-strand101-10661
β-strand128-13252
α-helix135-1395
β-strand142-15091
β-strand15613
β-strand159-16792
β-strand170-17892
α-helix1811
β-strand18213
α-helix1831
β-strand187-19591
α-helix196-1983
α-helix201-2099
β-strand214-22292
β-strand225-235112
Chain G: 5 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix62-654
α-helix79-813
β-strand87-9594
β-strand101-10664
β-strand128-13255
α-helix135-1395
β-strand142-151104
β-strand156-167125
β-strand170-182135
β-strand186-195104
α-helix196-1983
α-helix201-2099
β-strand214-22295
β-strand225-235115
Chain J: 7 helices, 11 β-strands
ElementResiduesLengthSheet
α-helix62-643
α-helix79-813
β-strand87-9596
β-strand101-10666
β-strand128-13257
α-helix135-1395
β-strand142-151106
β-strand15618
β-strand159-16797
β-strand170-17897
α-helix1811
β-strand18218
α-helix1831
β-strand186-195106
α-helix196-1983
α-helix201-2099
β-strand214-22297
β-strand225-235117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein unc-119 homolog ADprotein182Homo sapiensQ13432 (AlphaFold model)
Gly-cys-gly-cys-ser-serE, H, Kprotein10Homo sapiensP06239 (AlphaFold model)
Protein unc-119 homolog AG, Jprotein182Homo sapiensQ13432 (AlphaFold model)
Sequence of entity 1 (D), FASTA
>6H6A_1 Protein unc-119 homolog A (chains D)
PIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINR
RDKDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFH
FGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSG
TP
Sequence of entity 2 (E, H, K), FASTA
>6H6A_2 GLY-CYS-GLY-CYS-SER-SER (chains E, H, K)
GCGCSSHPED
Sequence of entity 3 (G, J), FASTA
>6H6A_3 Protein unc-119 homolog A (chains G, J)
PIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINR
RDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFH
FGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSG
TP

Ligands and cofactors

IDNameFormulaCopies
15PPolyethylene glycol (N=34)C69 H140 O351
MYRMyristic acidC14 H28 O23
PO4Phosphate ionO4 P2

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

Primary citation

The Ciliary Machinery Is Repurposed for T Cell Immune Synapse Trafficking of LCK. Stephen, L.A., ElMaghloob, Y., McIlwraith, M.J. et al. Dev Cell (2018) 47:122-132.e4. DOI 10.1016/j.devcel.2018.08.012 · PubMed

Other PDB entries of the same protein (UniProt Q13432 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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