Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF. Determined by X-ray diffraction at 2.5 Å resolution. Released 14 Dec 2004.
Explore 1XCG in 3D Show helices and sheets RCSB PDB PDBe
1XCG contains 58 α-helices and 33 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 | 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 | 819-833 | 15 | |
| 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 | 901-939 | 39 | |
| β-strand | 940-941 | 2 | 1 |
| α-helix | 943-946 | 4 | |
| α-helix | 954-958 | 5 | |
| α-helix | 961-963 | 3 | |
| β-strand | 966-974 | 9 | 1 |
| β-strand | 983-989 | 7 | 1 |
| β-strand | 992-998 | 7 | 1 |
| β-strand | 1003-1004 | 2 | 1 |
| β-strand | 1025-1027 | 3 | 1 |
| α-helix | 1028-1030 | 3 | |
| β-strand | 1031-1035 | 5 | 1 |
| β-strand | 1042-1047 | 6 | 1 |
| β-strand | 1056-1060 | 5 | 1 |
| α-helix | 1064-1080 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 2 |
| α-helix | 18-27 | 10 | |
| β-strand | 42-48 | 7 | 2 |
| β-strand | 51-58 | 8 | 2 |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 2 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 2 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-133 | 9 | |
| α-helix | 141-150 | 10 | |
| β-strand | 155-158 | 4 | 2 |
| α-helix | 167-179 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 716-718 | 3 | |
| 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 | 901-937 | 37 | |
| β-strand | 940-941 | 2 | 3 |
| α-helix | 951-954 | 4 | |
| 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 | 4 |
| β-strand | 1022 | 1 | 4 |
| β-strand | 1025-1027 | 3 | 3 |
| α-helix | 1028-1030 | 3 | |
| β-strand | 1031-1035 | 5 | 3 |
| β-strand | 1042-1047 | 6 | 3 |
| α-helix | 1053-1054 | 2 | |
| β-strand | 1055-1060 | 6 | 3 |
| α-helix | 1064-1080 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-11 | 8 | 5 |
| α-helix | 18-26 | 9 | |
| β-strand | 42-48 | 7 | 5 |
| β-strand | 51-58 | 8 | 5 |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 5 |
| β-strand | 88 | 1 | 5 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-132 | 8 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-150 | 10 | |
| β-strand | 155-158 | 4 | 5 |
| α-helix | 167-179 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho guanine nucleotide exchange factor 11 | A, E | protein | 368 | Homo sapiens | O15085 (AlphaFold model) |
| Transforming protein RhoA | B, F | protein | 178 | Homo sapiens | P61586 (AlphaFold model) |
>1XCG_1 Rho guanine nucleotide exchange factor 11 (chains A, E) QNWQHTVGKDVVAGLTQREIDRQEVINELFVTEASHLRTLRVLDLIFYQRMKKENLMPRE ELARLFPNLPELIEIHNSWCEAMKKLREEGPIIKEISDLMLARFDGPAREELQQVAAQFC SYQSIALELIKTKQRKESRFQLFMQEAESHPQCRRLQLRDLIISEMQRLTKYPLLLESII KHTEGGTSEHEKLCRARDQCREILKYVNEAVKQTENRHRLEGYQKRLDATALERASNPLA AEFKSLDLTTRKMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCHSKTAV GSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKNTWMEL LEEAVRNA
>1XCG_2 Transforming protein RhoA (chains B, F) AIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAG QEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLR NDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
The crystal structure of RhoA in complex with the DH/PH fragment of PDZRhoGEF, an activator of the Ca(2+) sensitization pathway in smooth muscle. Derewenda, U., Oleksy, A., Stevenson, A.S. et al. Structure (2004) 12:1955-1965. DOI 10.1016/j.str.2004.09.003 · PubMed
Other PDB entries of the same protein (UniProt O15085 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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