Research workbench
H-RAS complexed with diaminobenzophenone-BETA,GAMMA-imido-GTP
Analyse H-RAS complexed with diaminobenzophenone-BETA,GAMMA-imido-GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RVD
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming protein P21/H-RAS-1
- UniProt
- P01112
- Ligands
- DBG, MG
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming protein P21/H-RAS-1 | protein | 160 | 36% helix, 26% strand | P01112 |
Ligands and binding sites
- DBG · 3-aminobenzophenone-4-yl-aminohydroxyphosphinylaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RVD · H-RAS complexed with diaminobenzophenone-BETA,GAMMA-imido-GTP · 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 1RVD · PDBe 1RVD · UniProt P01112
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