Research workbench
C-H-RAS P21 protein mutant with thr 35 replaced by ser (T35S) complexed with guanosine-5'-[B,G-imido] triphosphate
Analyse C-H-RAS P21 protein mutant with thr 35 replaced by ser (T35S) complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IAQ
- Type
- protein
- Length
- 453 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein P21/H-RAS-1
- UniProt
- P01112
- Ligands
- GNP, MG
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein P21/H-RAS-1 | protein | 149 | 30% helix, 26% strand | P01112 |
| B | Transforming protein P21/H-RAS-1 | protein | 151 | 32% helix, 25% strand | P01112 |
| C | Transforming protein P21/H-RAS-1 | protein | 153 | 29% helix, 24% strand | P01112 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 794 | 0.75 | 0.80 | 66 | empty |
| 2 | 189 | 0.53 | 0.78 | 33 | empty |
| 3 | 51 | 0.33 | 0.78 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–B · 896 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 258 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 172 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1IAQ · C-H-RAS P21 protein mutant with thr 35 replaced by ser (T35S) complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01112
- Elsewhere: RCSB PDB 1IAQ · PDBe 1IAQ · UniProt P01112
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