Research workbench
NMR structure of the RAD53 FHA1 domain in complex with a phosphothreonien peptide derived from RAD53 SCD1
Analyse NMR structure of the RAD53 FHA1 domain in complex with a phosphothreonien… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JQI
- Type
- protein
- Length
- 161 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22216
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 151 | — | P22216 |
| B | — | protein | 10 | — | P22216 |
Compared structures
- 2JQI · NMR Structure of the Rad53 FHA1 domain in complex with a phosphothreonien peptide derived… · the same entry in another collection · chain A against A, TM-score 1.00
- P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · 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 P22216
- Elsewhere: RCSB PDB 2JQI · PDBe 2JQI · UniProt P22216
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