Crystal Structure of RhoA-GDP-Pi in Complex with RhoGAP. Determined by X-ray diffraction at 1.75 Å resolution. Released 8 May 2019.
Explore 6R3V in 3D Show helices and sheets RCSB PDB PDBe
6R3V contains 27 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 | 49-55 | 7 | |
| α-helix | 64-76 | 13 | |
| α-helix | 90-101 | 12 | |
| α-helix | 108-110 | 3 | |
| α-helix | 115-127 | 13 | |
| α-helix | 135-137 | 3 | |
| α-helix | 138-142 | 5 | |
| α-helix | 144-146 | 3 | |
| α-helix | 149-151 | 3 | |
| α-helix | 152-160 | 9 | |
| α-helix | 165-183 | 19 | |
| α-helix | 185-188 | 4 | |
| α-helix | 192-203 | 12 | |
| α-helix | 209-214 | 6 | |
| α-helix | 216-228 | 13 | |
| α-helix | 230-233 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-12 | 9 | 1 |
| α-helix | 18-23 | 6 | |
| β-strand | 40-48 | 9 | 1 |
| β-strand | 51-59 | 9 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 70-73 | 4 | |
| β-strand | 79-85 | 7 | 1 |
| α-helix | 89-94 | 6 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-106 | 7 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 119-121 | 3 | |
| α-helix | 125-132 | 8 | |
| α-helix | 138-140 | 3 | |
| α-helix | 141-151 | 11 | |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 167-179 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho GTPase-activating protein 1 | A | protein | 439 | Homo sapiens | Q07960 (AlphaFold model) |
| Transforming protein RhoA | B | protein | 193 | Homo sapiens | P61586 (AlphaFold model) |
>6R3V_1 Rho GTPase-activating protein 1 (chains A) MDPLSELQDDLTLDDTSEALNQLKLASIDEKNWPSDEMPDFPKSDDSKSSSPELVTHLKW DDPYYDIARHQIVEVAGDDKYGRKIIVFSACRMPPSHQLDHSKLLGYLKHTLDQYVESDY TLLYLHHGLTSDNKPSLSWLRDAYREFDRKYKKNIKALYIVHPTMFIKTLLILFKPLISF KFGQKIFYVNYLSELSEHVKLEQLGIPRQVLKYDDFLKSTQKSPATAPKPMPPRPPLPNQ QFGVSLQHLQEKNPEQEPIPIVLRETVAYLQAHALTTEGIFRRSANTQVVREVQQKYNMG LPVDFDQYNELHLPAVILKTFLRELPEPLLTFDLYPHVVGFLNIDESQRVPATLQVLQTL PEENYQVLRFLTAFLVQISAHSDQNKMTNTNLAVVFGPNLLWAKDAAITLKAINPINTFT KFLLDHQGELFPSPDPSGL
>6R3V_2 Transforming protein RhoA (chains B) MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ ARRGKKKSGCLVL
| ID | Name | Formula | Copies |
|---|---|---|---|
| DTT | 2,3-dihydroxy-1,4-dithiobutane | C4 H10 O2 S2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| PO4 | Phosphate ion | O4 P | 2 |
Water and common crystallization additives (MES) are not listed.
A GAP-GTPase-GDP-PiIntermediate Crystal Structure Analyzed by DFT Shows GTP Hydrolysis Involves Serial Proton Transfers. Molt Jr., R.W., Pellegrini, E., Jin, Y. Chemistry (2019) 25:8484-8488. DOI 10.1002/chem.201901627 · PubMed
Other PDB entries of the same protein (UniProt Q07960 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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