Crystal structure of RhoGDI Glu(154,155)Ala mutant. Determined by X-ray diffraction at 1.3 Å resolution. Released 11 Dec 2002.
Explore 1KMT in 3D Show helices and sheets RCSB PDB PDBe
1KMT contains 9 α-helices and 23 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 |
|---|---|---|---|
| β-strand | 66 | 1 | 1 |
| α-helix | 67-68 | 2 | |
| β-strand | 70-78 | 9 | 2 |
| β-strand | 87-89 | 3 | 2 |
| α-helix | 94-99 | 6 | |
| β-strand | 102-105 | 4 | 3 |
| β-strand | 109-110 | 2 | 4 |
| β-strand | 111-118 | 8 | 2 |
| β-strand | 123-134 | 12 | 3 |
| β-strand | 137-149 | 13 | 3 |
| α-helix | 155 | 1 | |
| β-strand | 156-159 | 4 | 2 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 4 |
| β-strand | 173-182 | 10 | 3 |
| β-strand | 190-199 | 10 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 66-68 | 3 | |
| β-strand | 70-78 | 9 | 1 |
| β-strand | 87-89 | 3 | 1 |
| α-helix | 94-99 | 6 | |
| β-strand | 102-105 | 4 | 5 |
| β-strand | 109-110 | 2 | 6 |
| β-strand | 111-118 | 8 | 1 |
| β-strand | 123-134 | 12 | 5 |
| β-strand | 137-149 | 13 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 156-159 | 4 | 1 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 6 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-182 | 10 | 5 |
| β-strand | 190-199 | 10 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho GDP-dissociation inhibitor 1 | A, B | protein | 141 | Homo sapiens | P52565 (AlphaFold model) |
>1KMT_1 Rho GDP-dissociation inhibitor 1 (chains A, B) GAMVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIV SGMKYIQHTYRKGVKIDKTDYMVGSYGPRAAAYEFLTPVEEAPKGMLARGSYSIKSRFTD DDKTDHLSWEWNLTIKKDWKD
The impact of Glu-->Ala and Glu-->Asp mutations on the crystallization properties of RhoGDI: the structure of RhoGDI at 1.3 A resolution. Mateja, A., Devedjiev, Y., Krowarsch, D. et al. Acta Crystallogr D Biol Crystallogr (2002) 58:1983-1991. DOI 10.1107/S090744490201394X · PubMed
Other PDB entries of the same protein (UniProt P52565 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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