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The crystal structure of REM1 in complex with GDP
Analyse The crystal structure of REM1 in complex with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NZJ
- Type
- protein
- Length
- 629 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein rem 1
- UniProt
- O75628
- Ligands
- GDP, MG, CL
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding protein rem 1 | protein | 155 | 37% helix, 27% strand | O75628 |
| B | GTP-binding protein rem 1 | protein | 160 | 38% helix, 26% strand | O75628 |
| C | GTP-binding protein rem 1 | protein | 159 | 34% helix, 27% strand | O75628 |
| D | GTP-binding protein rem 1 | protein | 155 | 38% helix, 27% strand | O75628 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.63 | 0.90 | 23 | empty |
| 2 | 168 | 0.60 | 0.83 | 37 | empty |
| 3 | 216 | 0.57 | 0.80 | 30 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1047 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 812 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 533 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 O75628
- Elsewhere: RCSB PDB 2NZJ · PDBe 2NZJ · UniProt O75628
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