Research workbench
Human CtBP1 (28-375) in complex with AMP
Analyse Human CtBP1 (28-375) in complex with AMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V8A
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- Source
- Homo sapiens
- Molecule
- C-terminal-binding protein 1
- EC
- 1.1.1.-
- UniProt
- Q13363
- Ligands
- AMP, CA, CL
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · resolution 2.35 · 1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-terminal-binding protein 1 (EC 1.1.1.-) | protein | 332 | 35% helix, 17% strand | Q13363 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.70 | 0.81 | 51 | AMP, CL |
| 2 | 74 | 0.33 | 0.75 | 17 | empty |
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 Q13363
- Elsewhere: RCSB PDB 6V8A · PDBe 6V8A · UniProt Q13363
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