Canine GDP-ran Q69L mutant. Determined by X-ray diffraction at 2.15 Å resolution. Released 2 Dec 1998.
Explore 3RAN in 3D Show helices and sheets RCSB PDB PDBe
3RAN contains 49 α-helices and 48 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 |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 23-28 | 6 | |
| β-strand | 30 | 1 | 2 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 1 |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-112 | 12 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| β-strand | 145-149 | 5 | 1 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-178 | 3 | 1 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 2 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-204 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-16 | 7 | 4 |
| α-helix | 23-27 | 5 | |
| β-strand | 30 | 1 | 5 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 4 |
| β-strand | 45-54 | 10 | 4 |
| β-strand | 57-66 | 10 | 4 |
| α-helix | 70-71 | 2 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 4 |
| α-helix | 95-111 | 17 | |
| β-strand | 117-122 | 6 | 4 |
| α-helix | 133-135 | 3 | |
| β-strand | 144-149 | 6 | 4 |
| β-strand | 150 | 1 | 6 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 6 |
| α-helix | 158-169 | 12 | |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 5 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-204 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-16 | 7 | 7 |
| α-helix | 23-27 | 5 | |
| β-strand | 30 | 1 | 8 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 7 |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 7 |
| β-strand | 57-66 | 10 | 7 |
| α-helix | 70-71 | 2 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 7 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-112 | 12 | |
| β-strand | 117-122 | 6 | 7 |
| α-helix | 133-138 | 6 | |
| β-strand | 144-148 | 5 | 7 |
| β-strand | 150 | 1 | 9 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 9 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-178 | 3 | 7 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 8 |
| α-helix | 191-205 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| β-strand | 10-16 | 7 | 10 |
| α-helix | 23-28 | 6 | |
| β-strand | 30 | 1 | 11 |
| α-helix | 31-35 | 5 | |
| β-strand | 38-40 | 3 | 10 |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 10 |
| β-strand | 57-66 | 10 | 10 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 10 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 10 |
| α-helix | 133-136 | 4 | |
| β-strand | 144-148 | 5 | 10 |
| β-strand | 150 | 1 | 12 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 12 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-178 | 3 | 10 |
| α-helix | 179-181 | 3 | |
| β-strand | 182 | 1 | 11 |
| α-helix | 183-185 | 3 | |
| α-helix | 191-205 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (GTP-binding nuclear protein ran) | A, B, C, D | protein | 216 | Canis lupus familiaris | P62825 (AlphaFold model) |
>3RAN_1 PROTEIN (GTP-BINDING NUCLEAR PROTEIN RAN) (chains A, B, C, D) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2). Stewart, M., Kent, H.M., McCoy, A.J. J Mol Biol (1998) 284:1517-1527. DOI 10.1006/jmbi.1998.2204 · PubMed
Other PDB entries of the same protein (UniProt P62825 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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