Research workbench
Solution structure of the brct domain from human replication factor C large subunit 1
Analyse Solution structure of the brct domain from human replication factor C large… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EBU
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Replication factor C subunit 1
- UniProt
- P35251
- Pockets
- 1 · best druggability 0.31
Structure
solution nmr · 1 distinct chain · 26% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication factor C subunit 1 | protein | 112 | 26% helix, 13% strand | P35251 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.31 | 0.74 | 19 | empty |
Compared structures
- 2EBU · Solution structure of the BRCT domain from human replication factor C large subunit 1 · the same entry in another collection · chain A against A, TM-score 1.00
- P35251 · AlphaFold monomer V2.0 prediction for replication factor C subunit 1 (P35251) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P35251
- Elsewhere: RCSB PDB 2EBU · PDBe 2EBU · UniProt P35251
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.