Research workbench
Crystal structure of the RAS homolog domain of human GRLF1 (P190RHOGAP)
Analyse Crystal structure of the RAS homolog domain of human GRLF1 (P190RHOGAP) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C5H
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucocorticoid receptor DNA-binding factor 1
- UniProt
- Q9NRY4
- Ligands
- GNP, MG, UNX
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucocorticoid receptor DNA-binding factor 1 | protein | 232 | 32% helix, 23% strand | Q9NRY4 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- UNX · Unknown atom or ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.56 | 0.81 | 31 | MG, GNP |
| 2 | 63 | 0.31 | 0.75 | 16 | empty |
| 3 | 53 | 0.25 | 0.73 | 15 | empty |
Compared structures
- 3C5H · Crystal structure of the Ras homolog domain of human GRLF1 (p190RhoGAP) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NRY4 · AlphaFold monomer V2.0 prediction for rho GTPase-activating protein 35 (Q9NRY4) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9NRY4
- Elsewhere: RCSB PDB 3C5H · PDBe 3C5H · UniProt Q9NRY4
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