2DWX: ADP-ribosylation factor-binding protein GGA1

Co-crystal Structure Analysis of GGA1-GAE with the WNSF motif. Determined by X-ray diffraction at 2.55 Å resolution. Released 17 Apr 2007.

Method: X-ray diffraction
Resolution: 2.55 Å
Organism: Homo sapiens
Chains: 6
Atoms: 4,235
Mol. weight: 62.34 kDa
Released: 17 Apr 2007

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

Secondary structure: helices and β-sheets

2DWX contains 13 α-helices and 45 β-strands across 6 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: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	514	1
β-strand	515-520	6	1
β-strand	523-531	9	1
β-strand	540-549	10	1
β-strand	555-563	9	2
β-strand	565	1	3
β-strand	569-572	4	1
α-helix	573-575	3
β-strand	580	1	2
α-helix	581-583	3
α-helix	588-590	3
β-strand	592-599	8	1
β-strand	608-616	9	2
β-strand	619-627	9	2
α-helix	630-632	3
α-helix	633-636	4

Chain B: 1 helix, 10 β-strands

Element	Residues	Length	Sheet
β-strand	515-520	6	4
β-strand	523-529	7	4
β-strand	543-549	7	4
β-strand	555	1	5
β-strand	556-561	6	6
β-strand	572	1	4
β-strand	580	1	5
β-strand	592-596	5	4
β-strand	610-615	6	6
β-strand	620-625	6	6
α-helix	630-632	3

Chain C: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	515-520	6	7
β-strand	523-531	9	7
β-strand	540-549	10	7
β-strand	555	1	8
β-strand	556-563	8	9
β-strand	565	1	10
β-strand	569-572	4	7
α-helix	573-575	3
β-strand	580	1	8
α-helix	588-590	3
β-strand	592-599	8	7
α-helix	604-606	3
β-strand	608-615	8	9
β-strand	620-627	8	9

Chain D: 3 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	515-520	6	11
β-strand	523-530	8	11
β-strand	540-548	9	11
β-strand	555	1	12
β-strand	556-563	8	13
β-strand	569-572	4	11
α-helix	573-575	3
β-strand	580	1	12
β-strand	592-599	8	11
β-strand	608-615	8	13
β-strand	620-627	8	13
α-helix	630-632	3
α-helix	633-638	6

Chains P and Q: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	0	1	3
β-strand	4	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ADP-ribosylation factor-binding protein GGA1	A, B, C, D	protein	133	Homo sapiens	Q9UJY5 (AlphaFold model)
hinge peptide from ADP-ribosylation factor binding protein GGA1	P, Q	protein	13		Q9UJY5 (AlphaFold model)

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

>2DWX_1 ADP-ribosylation factor-binding protein GGA1 (chains A, B, C, D)
IKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVVSMLSTAPQPIRNIVFQSAVPK
VMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEKVRLRYKLTFTMGDQTYNEMGD
VDQFPPPETWGSL

Sequence of entity 2 (P, Q), FASTA

>2DWX_2 hinge peptide from ADP-ribosylation factor binding protein GGA1 (chains P, Q)
SLDGTGWNSFQSS

Primary citation

Molecular Basis for Autoregulatory Interaction Between GAE Domain and Hinge Region of GGA1. Inoue, M., Shiba, T., Ihara, K. et al. Traffic (2007) 8:904-913. DOI 10.1111/j.1600-0854.2007.00577.x · PubMed

Other PDB entries of the same protein (UniProt Q9UJY5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1J2J 1.6 Å, Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form
3G2S 1.7 Å, VHS Domain of human GGA1 complexed with SorLA C-terminal Peptide
1UJK 1.9 Å, VHS domain of human GGA1 complexed with C-terminal phosphopeptide from BACE
1JWG 2.0 Å, VHS Domain of human GGA1 complexed with cation-independent M6PR C-terminal Peptide
3G2T 2.0 Å, VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide
1JWF 2.1 Å, Crystal Structure of human GGA1 VHS domain.
1O3X 2.1 Å, Crystal structure of human GGA1 GAT domain
3G2V 2.1 Å, VHS Domain of human GGA1 complexed with Sotilin C-terminal Phosphopeptide
1NA8 2.3 Å, Crystal structure of ADP-ribosylation factor binding protein GGA1
2DWY 2.3 Å, Crystal Structure Analysis of GGA1-GAE
3G2U 2.3 Å, VHS Domain of human GGA1 complexed with Sotilin C-terminal Peptide
1NWM 2.4 Å, GAT domain of human GGA1

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