1OM9: GGA1-appendage

Structure of the GGA1-appendage in complex with the p56 binding peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 29 Jul 2003.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,446
Mol. weight: 37.95 kDa
Released: 29 Jul 2003

Explore 1OM9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OM9 contains 14 α-helices and 24 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: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	504-506	3
α-helix	507-509	3
α-helix	513-514	2
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	591-599	9	1
α-helix	604-606	3
β-strand	608-616	9	2
β-strand	619-627	9	2

Chain B: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	504-506	3
α-helix	513-514	2
β-strand	515-520	6	4
β-strand	523-531	9	4
β-strand	540-549	10	4
β-strand	555-563	9	5
β-strand	565	1	6
β-strand	569-575	7	4
β-strand	580	1	5
α-helix	581-583	3
α-helix	588-590	3
β-strand	591-599	9	4
α-helix	604-606	3
β-strand	608-616	9	5
β-strand	619-627	9	5

Chains P and Q: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	3
α-helix	7-8	2
β-strand	9	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ADP-ribosylation factor binding protein GGA1	A, B	protein	154	Homo sapiens	Q9UJY5 (AlphaFold model)
15-mer peptide fragment of p56	P, Q	protein	15		Q7Z6B0 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1OM9_1 ADP-ribosylation factor binding protein GGA1 (chains A, B)
MHHHHHHMELSLASITVPLESIKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVV
SMLSTAPQPIRNIVFQSAVPKVMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEK
VRLRYKLTFTMGDQTYNEMGDVDQFPPPETWGSL

Sequence of entity 2 (P, Q), FASTA

>1OM9_2 15-mer peptide fragment of p56 (chains P, Q)
DDDDFGGFEAAETFD

Primary citation

Structural basis for binding of accessory proteins by the appendage domain of GGAs. Collins, B.M., Praefcke, G.J.K., Robinson, M.S. et al. Nat Struct Biol (2003) 10:607-613. DOI 10.1038/nsb955 · 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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