2J59: ARF1:ARHGAP21-ArfBD complex

Crystal structure of the ARF1:ARHGAP21-ArfBD complex. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Feb 2007.

Method: X-ray diffraction
Resolution: 2.1 Å
Organisms: MUS MUSCULUS, HOMO SAPIENS
Chains: 12
Atoms: 15,535
Mol. weight: 234.3 kDa
Ligands: GTP, MG, DIO
Released: 20 Feb 2007

Explore 2J59 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2J59 contains 68 α-helices and 86 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: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	1
α-helix	30-39	10
β-strand	51-58	8	1
β-strand	61-68	8	1
α-helix	72-81	10
β-strand	87-93	7	1
α-helix	100-111	12
α-helix	114-116	3
β-strand	120-126	7	1
α-helix	133-135	3
α-helix	136-143	8
α-helix	145-147	3
β-strand	153-157	5	1
β-strand	159	1	2
β-strand	164	1	2
α-helix	166-178	13

Chain B: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	3
α-helix	30-39	10
β-strand	51-58	8	3
β-strand	61-68	8	3
α-helix	72-81	10
β-strand	87-93	7	3
α-helix	97-99	3
α-helix	100-110	11
α-helix	114-116	3
β-strand	120-126	7	3
α-helix	133-135	3
α-helix	136-142	7
α-helix	145-147	3
β-strand	153-157	5	3
α-helix	166-179	14

Chains C and F: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	4
α-helix	30-39	10
β-strand	51-58	8	4
β-strand	61-68	8	4
α-helix	72-81	10
β-strand	87-93	7	4
α-helix	100-111	12
α-helix	114-116	3
β-strand	120-126	7	4
α-helix	133-135	3
α-helix	136-142	7
α-helix	145-147	3
β-strand	153-157	5	4
β-strand	159	1	5
β-strand	164	1	5
α-helix	166-178	13

Chain D: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	6
α-helix	30-39	10
β-strand	51-58	8	6
β-strand	61-68	8	6
α-helix	72-81	10
β-strand	87-93	7	6
α-helix	97-99	3
α-helix	100-111	12
α-helix	114-116	3
β-strand	120-126	7	6
α-helix	133-135	3
α-helix	136-143	8
α-helix	145-147	3
β-strand	153-157	5	6
α-helix	166-179	14

Chain E: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	7
α-helix	30-39	10
β-strand	51-58	8	7
β-strand	61-68	8	7
α-helix	72-81	10
β-strand	87-93	7	7
α-helix	97-99	3
α-helix	100-111	12
α-helix	114-116	3
β-strand	120-126	7	7
α-helix	133-135	3
α-helix	136-142	7
α-helix	145-147	3
β-strand	153-157	5	7
β-strand	159	1	8
β-strand	164	1	8
α-helix	166-178	13

Chain M: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	933-941	9	11
β-strand	958-965	8	11
β-strand	968-972	5	11
β-strand	988-989	2	11
β-strand	994-997	4	11
β-strand	1007-1011	5	11
β-strand	1016-1020	5	11
α-helix	1024-1037	14
α-helix	1042-1062	21

Chain N: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	933-941	9	12
β-strand	958-965	8	12
β-strand	968-972	5	12
β-strand	988-989	2	12
β-strand	994-997	4	12
β-strand	1007-1011	5	12
β-strand	1016-1020	5	12
α-helix	1024-1036	13
α-helix	1042-1062	21

Chain O: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	933-941	9	13
β-strand	958-965	8	13
β-strand	968-972	5	13
β-strand	988-989	2	13
β-strand	994-997	4	13
β-strand	1007-1011	5	13
β-strand	1016-1020	5	13
α-helix	1024-1036	13
α-helix	1042-1060	19

3 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
ADP-ribosylation factor 1	A, B, C, D, E, F	protein	166	MUS MUSCULUS	P84078 (AlphaFold model)
Rho-gtpase activating protein 10	M, N, O, P, Q, R	protein	168	HOMO SAPIENS	Q5T5U3 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>2J59_1 ADP-RIBOSYLATION FACTOR 1 (chains A, B, C, D, E, F)
GSMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGLDKIR
PLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMN
AAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK

Sequence of entity 2 (M, N, O, P, Q, R), FASTA

>2J59_2 RHO-GTPASE ACTIVATING PROTEIN 10 (chains M, N, O, P, Q, R)
SDAAKEGWLHFRPLVTDKGKRVGGSIRPWKQMYVVLRGHSLYLYKDKREQTTPSEEEQPI
SVNACLIDISYSETKRKNVFRLTTSDCECLFQAEDRDDMLAWIKTIQESSNLNEEDTGVT
NRDLISRRIKEYNNLMSKAEQLPKTPRQSLSIRQTLLGAKSEPKTQSP

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	6
MG	Magnesium ion	Mg	6
DIO	1,4-diethylene dioxide	C4 H8 O2	3

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

Primary citation

Structural Basis for Arf1-Mediated Recruitment of Arhgap21 to Golgi Membranes. Menetrey, J., Perderiset, M., Cicolari, J. et al. EMBO J (2007) 26:1953. DOI 10.1038/SJ.EMBOJ.7601634 · PubMed

Other PDB entries of the same protein (UniProt P84078 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1O3Y 1.5 Å, Crystal structure of mouse ARF1 (delta17-Q71L), GTP form
1J2J 1.6 Å, Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form

Browse structure collections

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