4GOK: Arl2GppNHp

The Crystal structure of Arl2GppNHp in complex with UNC119a. Determined by X-ray diffraction at 2.6 Å resolution. Released 19 Sept 2012.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Mus musculus, Homo sapiens
Chains: 4
Atoms: 5,234
Mol. weight: 93.23 kDa
Ligands: GNP, MG
Released: 19 Sept 2012

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

Secondary structure: helices and β-sheets

4GOK contains 26 α-helices and 34 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: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	18-22	5	4
α-helix	29-35	7
β-strand	50-57	8	4
β-strand	60-67	8	4
α-helix	74-80	7
β-strand	86-92	7	4
α-helix	96-98	3
α-helix	99-110	12
α-helix	113-115	3
β-strand	119-125	7	4
α-helix	132-134	3
α-helix	135-142	8
α-helix	144-146	3
β-strand	152-156	5	4
β-strand	158	1	5
β-strand	163	1	5
α-helix	166-178	13

Chain B: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	18-22	5	1
α-helix	29-35	7
β-strand	50-57	8	1
β-strand	60-67	8	1
α-helix	74-80	7
β-strand	86-92	7	1
α-helix	96-98	3
α-helix	99-110	12
α-helix	113-115	3
β-strand	119-125	7	1
α-helix	132-134	3
α-helix	135-141	7
α-helix	144-146	3
β-strand	152-156	5	1
β-strand	158	1	2
β-strand	163	1	2
α-helix	166-178	13

Chains C and G: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	62-66	5
α-helix	79-81	3
β-strand	87-95	9	4
β-strand	101-106	6	4
β-strand	128-132	5	6
α-helix	135-139	5
β-strand	143-150	8	4
β-strand	156-167	12	6
β-strand	170-182	13	6
β-strand	187-193	7	4
α-helix	201-209	9
β-strand	214-222	9	6
β-strand	225-235	11	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ADP-ribosylation factor-like protein 2	A, B	protein	169	Mus musculus	Q9D0J4 (AlphaFold model)
Protein unc-119 homolog A	C, G	protein	240	Homo sapiens	Q13432 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4GOK_1 ADP-ribosylation factor-like protein 2 (chains A, B)
MLRLLMLGLDNAGKTTILKKFNGEDVDTISPTLGFNIKTLEHRGFKLNIWDVGGLKSLRS
YWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSC
NAIQEALELDSIRSHHWRIQGCSAVTGEDLLPGIDWLLDDISSRVFTAD

Sequence of entity 2 (C, G), FASTA

>4GOK_2 Protein unc-119 homolog A (chains C, G)
MKVKKGGGGAGTATESAPGPSGQSVAPIPQPPAESESGSESEPDAGPGPRPGPLQRKQPI
GPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINRRD
LDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFG
FCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

Structural basis for Arl3-specific release of myristoylated ciliary cargo from UNC119. Ismail, S.A., Chen, Y.X., Miertzschke, M. et al. EMBO J (2012) 31:4085-4094. DOI 10.1038/emboj.2012.257 · PubMed

Other PDB entries of the same protein (UniProt Q9D0J4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KSH 1.8 Å, Complex of Arl2 and PDE delta, Crystal Form 2 (native)
1KSG 2.3 Å, Complex of Arl2 and PDE delta, Crystal Form 1
1KSJ 2.6 Å, Complex of Arl2 and PDE delta, Crystal Form 2 (SeMet)

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