Crystal structure of the complex between the human RhoA and the DH/PH domain of human ARHGEF11. Determined by X-ray diffraction at 2.5 Å resolution. Released 26 Apr 2017.
Explore 5JHG in 3D Show helices and sheets RCSB PDB PDBe
5JHG contains 55 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 730-755 | 26 | |
| α-helix | 756-761 | 6 | |
| α-helix | 762-766 | 5 | |
| α-helix | 772-778 | 7 | |
| α-helix | 782-801 | 20 | |
| α-helix | 810-817 | 8 | |
| α-helix | 820-833 | 14 | |
| α-helix | 836-849 | 14 | |
| α-helix | 851-861 | 11 | |
| α-helix | 864-866 | 3 | |
| α-helix | 871-875 | 5 | |
| α-helix | 877-894 | 18 | |
| α-helix | 901-938 | 38 | |
| β-strand | 940-941 | 2 | 1 |
| α-helix | 951-954 | 4 | |
| α-helix | 955-958 | 4 | |
| α-helix | 961-963 | 3 | |
| β-strand | 966-974 | 9 | 2 |
| β-strand | 983-989 | 7 | 2 |
| β-strand | 992-994 | 3 | 2 |
| β-strand | 997-999 | 3 | 1 |
| β-strand | 1002-1004 | 3 | 1 |
| β-strand | 1025-1027 | 3 | 2 |
| α-helix | 1028-1030 | 3 | |
| β-strand | 1031-1034 | 4 | 2 |
| β-strand | 1042-1047 | 6 | 2 |
| β-strand | 1055 | 1 | 3 |
| β-strand | 1057-1060 | 4 | 2 |
| α-helix | 1064-1080 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-12 | 8 | 4 |
| α-helix | 18-27 | 10 | |
| β-strand | 42-48 | 7 | 4 |
| β-strand | 51-58 | 8 | 4 |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 4 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-151 | 11 | |
| β-strand | 155-158 | 4 | 4 |
| α-helix | 167-179 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 725-727 | 3 | |
| α-helix | 730-755 | 26 | |
| α-helix | 756-761 | 6 | |
| α-helix | 762-766 | 5 | |
| α-helix | 772-778 | 7 | |
| α-helix | 782-801 | 20 | |
| α-helix | 810-817 | 8 | |
| α-helix | 820-833 | 14 | |
| α-helix | 836-849 | 14 | |
| α-helix | 851-861 | 11 | |
| α-helix | 864-866 | 3 | |
| α-helix | 871-874 | 4 | |
| α-helix | 877-894 | 18 | |
| α-helix | 901-938 | 38 | |
| β-strand | 940-941 | 2 | 3 |
| α-helix | 952-957 | 6 | |
| α-helix | 961-963 | 3 | |
| β-strand | 966-977 | 12 | 3 |
| β-strand | 980-989 | 10 | 3 |
| β-strand | 992-998 | 7 | 3 |
| β-strand | 1003-1004 | 2 | 3 |
| β-strand | 1008 | 1 | 5 |
| β-strand | 1022 | 1 | 5 |
| β-strand | 1025-1027 | 3 | 3 |
| α-helix | 1028-1030 | 3 | |
| β-strand | 1031-1035 | 5 | 3 |
| β-strand | 1043-1047 | 5 | 3 |
| β-strand | 1055-1060 | 6 | 3 |
| α-helix | 1064-1079 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 6 |
| α-helix | 18-27 | 10 | |
| β-strand | 42-48 | 7 | 6 |
| β-strand | 51-58 | 8 | 6 |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 6 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 6 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 141-151 | 11 | |
| β-strand | 155-158 | 4 | 6 |
| α-helix | 167-179 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho guanine nucleotide exchange factor 11 | A, E | protein | 369 | Homo sapiens | O15085 (AlphaFold model) |
| Transforming protein RhoA | B, F | protein | 181 | Homo sapiens | P61586 (AlphaFold model) |
>5JHG_1 Rho guanine nucleotide exchange factor 11 (chains A, E) MQNWQHTVGKDVVAGLTQREIDRQEVINELFVTEASHLRTLRVLDLIFYQRMKKENLMPR EELARLFPNLPELIEIHNSWCEAMKKLREEGPIIKEISDLMLARFDGPAREELQQVAAQF CSYQSIALELIKTKQRKESRFQLFMQEAESHPQCRRLQLRDLIISEMQRLTKYPLLLESI IKHTEGGTSEHEKLCRARDQCREILKYVNEAVKQTENRHRLEGYQKRLDATALERASNPL AAEFKSLDLTTRKMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCHSKTA VGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKNTWME LLEEAVRNA
>5JHG_2 Transforming protein RhoA (chains B, F) MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ A
Crystallization and preliminary X-ray crystallographic analysis of a small GTPase RhoA bound with its inhibitor and ARHGEF11. Wang, R., Yan, Z., Lv, Z. et al. To be published.
Other PDB entries of the same protein (UniProt O15085 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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