Structure of the NTF2:RanGDP complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 1 Jul 2015.
Explore 5BXQ in 3D Show helices and sheets RCSB PDB PDBe
5BXQ contains 47 α-helices and 48 β-strands across 5 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 | 6-24 | 19 | |
| α-helix | 26-32 | 7 | |
| β-strand | 33-41 | 9 | 1 |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 49-57 | 9 | |
| β-strand | 64-75 | 12 | 1 |
| β-strand | 81-91 | 11 | 1 |
| α-helix | 94-96 | 3 | |
| β-strand | 97-108 | 12 | 1 |
| β-strand | 111-121 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-24 | 19 | |
| α-helix | 26-32 | 7 | |
| β-strand | 38-41 | 4 | 2 |
| β-strand | 44-47 | 4 | 2 |
| α-helix | 49-57 | 9 | |
| β-strand | 64-75 | 12 | 2 |
| β-strand | 81-91 | 11 | 2 |
| α-helix | 95-96 | 2 | |
| β-strand | 97-107 | 11 | 2 |
| β-strand | 112-121 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-17 | 9 | 3 |
| α-helix | 23-28 | 6 | |
| β-strand | 30 | 1 | 4 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 3 |
| β-strand | 45-54 | 10 | 3 |
| β-strand | 57-66 | 10 | 3 |
| α-helix | 69-71 | 3 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 3 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 3 |
| α-helix | 133-136 | 4 | |
| β-strand | 144-148 | 5 | 3 |
| β-strand | 150 | 1 | 5 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 5 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 3 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 4 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-202 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 6 |
| α-helix | 23-27 | 5 | |
| β-strand | 30 | 1 | 7 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 6 |
| β-strand | 45-54 | 10 | 6 |
| β-strand | 57-66 | 10 | 6 |
| α-helix | 69-71 | 3 | |
| α-helix | 74-76 | 3 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 6 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 6 |
| α-helix | 133-136 | 4 | |
| β-strand | 144-148 | 5 | 6 |
| β-strand | 150 | 1 | 8 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 8 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-178 | 3 | 6 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 7 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-207 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-16 | 7 | 9 |
| α-helix | 23-27 | 5 | |
| β-strand | 30 | 1 | 10 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 9 |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 9 |
| β-strand | 57-66 | 10 | 9 |
| α-helix | 69-72 | 4 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 9 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 9 |
| β-strand | 144-148 | 5 | 9 |
| β-strand | 150 | 1 | 11 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 11 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-178 | 3 | 9 |
| β-strand | 182 | 1 | 10 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-206 | 16 | |
| α-helix | 208-211 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear transport factor 2 | A, B | protein | 127 | Rattus norvegicus | P61972 (AlphaFold model) |
| GTP-binding nuclear protein Ran | C, D, E | protein | 216 | Canis familiaris | P62825 (AlphaFold model) |
>5BXQ_1 Nuclear transport factor 2 (chains A, B) MGDKPIWEQIGSSFIQHYYQLFDNDRTQLGAIYIDASCLTWEGQQFQGKAAIVEKLSSLP FQKIQHSITAQDHQPTPDSCIISMVVGQLKADEDPIMGFHQMFLLKNINDAWVCTNDMFR LALHNFG
>5BXQ_2 GTP-binding nuclear protein Ran (chains C, D, E) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Water and common crystallization additives (SO4) are not listed.
Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. Stewart, M., Kent, H.M., McCoy, A.J. J Mol Biol (1998) 277:635-646. DOI 10.1006/jmbi.1997.1602 · PubMed
Other PDB entries of the same protein (UniProt P61972 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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