Research workbench
NMR structure of rcl in complex with gmp
Analyse NMR structure of rcl in complex with gmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KLH
- Type
- protein
- Length
- 304 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-myc-responsive protein rcl
- UniProt
- O35820
- Ligands
- 5GP
- Pockets
- 11 · best druggability 0.54
Structure
solution nmr · 1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | C-myc-responsive protein rcl | protein | 152 | 45% helix, 14% strand | O35820 |
Ligands and binding sites
- 5GP · Guanosine-5'-monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.54 | 0.83 | 26 | 5GP |
| 2 | 128 | 0.54 | 0.82 | 30 | 5GP |
| 3 | 137 | 0.48 | 0.78 | 17 | empty |
| 4 | 124 | 0.48 | 0.79 | 16 | empty |
| 5 | 78 | 0.45 | 0.81 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1367 Ų buried · 4 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 O35820
- Elsewhere: RCSB PDB 2KLH · PDBe 2KLH · UniProt O35820
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