Research workbench
Replication factor C adpnp complex
Analyse Replication factor C adpnp complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CHQ
- Type
- protein
- Length
- 939 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Replication factor C small subunit
- UniProt
- O28219
- Ligands
- ANP
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Replication factor C small subunit | protein | 313 | 53% helix, 9% strand | O28219 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 850 | 0.81 | 0.84 | 85 | ANP |
| 2 | 911 | 0.77 | 0.80 | 83 | empty |
| 3 | 657 | 0.73 | 0.80 | 55 | ANP |
| 4 | 129 | 0.71 | 0.91 | 29 | empty |
| 5 | 235 | 0.69 | 0.85 | 29 | ANP |
Interfaces
2 interfaces between chains.
- A–B · 1587 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1414 Ų buried · 11 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 O28219
- Elsewhere: RCSB PDB 2CHQ · PDBe 2CHQ · UniProt O28219
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