Research workbench
Solution structure of the C-terminal domain of human RPA32 complexed with UNG2(73-88)
Analyse Solution structure of the C-terminal domain of human RPA32 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DPU
- Type
- protein
- Length
- 85 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15927, P13051
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 69 | — | P15927 |
| B | — | protein | 16 | — | P13051 |
Compared structures
- 1DPU · Solution structure of the C-terminal domain of human RPA32 complexed with UNG2(73-88) · the same entry in another collection · chain A against A, TM-score 1.00
- P15927 · AlphaFold monomer V2.0 prediction for replication protein a 32 kda subunit (P15927) · a predicted model of the same protein · chain A against A, TM-score 0.86
- P13051 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P13051) · a predicted model of the same protein · chain B against A, TM-score 0.67
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 P15927
- Every structure of UniProt P13051
- Elsewhere: RCSB PDB 1DPU · PDBe 1DPU · UniProt P15927 · UniProt P13051
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