crystal structure of ARAP3 RhoGAP domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 Jun 2016.
Explore 5JD0 in 3D Show helices and sheets RCSB PDB PDBe
5JD0 contains 26 α-helices and 6 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 909-911 | 3 | |
| β-strand | 914 | 1 | 1 |
| β-strand | 920 | 1 | 1 |
| α-helix | 921-933 | 13 | |
| α-helix | 947-960 | 14 | |
| α-helix | 961-963 | 3 | |
| α-helix | 973-986 | 14 | |
| α-helix | 997-1004 | 8 | |
| α-helix | 1009-1020 | 12 | |
| α-helix | 1025-1043 | 19 | |
| α-helix | 1045-1048 | 4 | |
| α-helix | 1052-1064 | 13 | |
| α-helix | 1071-1082 | 12 | |
| α-helix | 1084-1087 | 4 | |
| α-helix | 1092-1106 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 909-911 | 3 | |
| β-strand | 914 | 1 | 2 |
| β-strand | 920 | 1 | 2 |
| α-helix | 921-933 | 13 | |
| α-helix | 947-960 | 14 | |
| α-helix | 961-963 | 3 | |
| β-strand | 968 | 1 | 3 |
| β-strand | 971 | 1 | 3 |
| α-helix | 973-986 | 14 | |
| α-helix | 997-1004 | 8 | |
| α-helix | 1009-1020 | 12 | |
| α-helix | 1025-1043 | 19 | |
| α-helix | 1045-1048 | 4 | |
| α-helix | 1052-1063 | 12 | |
| α-helix | 1071-1082 | 12 | |
| α-helix | 1084-1087 | 4 | |
| α-helix | 1092-1104 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 | A, B | protein | 211 | Homo sapiens | Q8WWN8 (AlphaFold model) |
>5JD0_1 Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (chains A, B) MGHHHHHHMGTGLQEQQMSRGDIPIIVDACISFVTQHGLRLEGVYRKGGARARSLRLLAE FRRDARSVKLRPGEHFVEDVTDTLKRFFRELDDPVTSARLLPRWREAAELPQKNQRLEKY KDVIGCLPRVNRRTLATLIGHLYRVQKCAALNQMCTRNLALLFAPSVFQTDGRGEHEVRV LQELIDGYISVFDIDSDQVAQIDLEVSLITT
Structural Basis for the Specific Recognition of RhoA by the Dual GTPase-activating Protein ARAP3. Bao, H., Li, F., Wang, C. et al. J Biol Chem (2016) 291:16709-16719. DOI 10.1074/jbc.M116.736140 · PubMed
Other PDB entries of the same protein (UniProt Q8WWN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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