Crystal structure of rhogdi K135T,K138T,K141T mutant. Determined by X-ray diffraction at 1.88 Å resolution. Released 8 May 2007.
Explore 2JHT in 3D Show helices and sheets RCSB PDB PDBe
2JHT contains 12 α-helices and 44 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 | 70-78 | 9 | 1 |
| β-strand | 87-89 | 3 | 1 |
| α-helix | 95-99 | 5 | |
| β-strand | 102-105 | 4 | 2 |
| β-strand | 109-110 | 2 | 3 |
| β-strand | 111-118 | 8 | 1 |
| β-strand | 123-134 | 12 | 2 |
| β-strand | 138-149 | 12 | 2 |
| β-strand | 152-159 | 8 | 1 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 3 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-182 | 10 | 2 |
| β-strand | 190-199 | 10 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 70-78 | 9 | 4 |
| β-strand | 87-89 | 3 | 4 |
| α-helix | 97-99 | 3 | |
| β-strand | 102-105 | 4 | 5 |
| β-strand | 109-110 | 2 | 6 |
| β-strand | 111-118 | 8 | 4 |
| β-strand | 123-133 | 11 | 5 |
| β-strand | 139-149 | 11 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 156-159 | 4 | 4 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 6 |
| β-strand | 173-182 | 10 | 5 |
| β-strand | 190-199 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 70-78 | 9 | 7 |
| β-strand | 87-89 | 3 | 7 |
| α-helix | 95-99 | 5 | |
| β-strand | 102-105 | 4 | 8 |
| β-strand | 109-110 | 2 | 9 |
| β-strand | 111-118 | 8 | 7 |
| β-strand | 123-134 | 12 | 8 |
| β-strand | 137-149 | 13 | 8 |
| α-helix | 155 | 1 | |
| β-strand | 156-159 | 4 | 7 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 9 |
| β-strand | 173-182 | 10 | 8 |
| β-strand | 190-199 | 10 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 70-78 | 9 | 10 |
| β-strand | 87-89 | 3 | 10 |
| α-helix | 94-97 | 4 | |
| β-strand | 102-105 | 4 | 11 |
| β-strand | 109-110 | 2 | 12 |
| β-strand | 111-118 | 8 | 10 |
| β-strand | 123-133 | 11 | 11 |
| β-strand | 138-149 | 12 | 11 |
| α-helix | 155 | 1 | |
| β-strand | 156-159 | 4 | 10 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-164 | 2 | 12 |
| β-strand | 173-182 | 10 | 11 |
| β-strand | 188-199 | 12 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho GDP-dissociation inhibitor 1 | A, B, C, D | protein | 138 | HOMO SAPIENS | P52565 (AlphaFold model) |
>2JHT_1 RHO GDP-DISSOCIATION INHIBITOR 1 (chains A, B, C, D) AMVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVS GMKYIQHTYRTGVTIDTTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDD DKTDHLSWEWNLTIKKDW
| ID | Name | Formula | Copies |
|---|---|---|---|
| LI | Lithium ion | Li | 1 |
Water and common crystallization additives (SO4) are not listed.
Protein Crystallization by Surface Entropy Reduction: Optimization of the Ser Strategy. Cooper, D.R., Boczek, T., Grelewska, K. et al. Acta Crystallogr D Biol Crystallogr (2007) 63:636. DOI 10.1107/S0907444907010931 · 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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