Research workbench
Crystal structure of full-length human rpa 14/32 heterodimer
Analyse Crystal structure of full-length human rpa 14/32 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PQA
- Type
- protein
- Length
- 483 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15927, P35244
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 128 | — | P15927 |
| B | — | protein | 114 | — | P35244 |
| C | — | protein | 127 | — | P15927 |
| D | — | protein | 114 | — | P35244 |
Compared structures
- 2PQA · Crystal Structure of Full-length Human RPA 14/32 Heterodimer · the same entry in another collection · chain D against D, TM-score 1.00
- P35244 · AlphaFold monomer V2.0 prediction for replication protein a 14 kda subunit (P35244) · a predicted model of the same protein · chain D against A, TM-score 0.99
- 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 0.95
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 P35244
- Elsewhere: RCSB PDB 2PQA · PDBe 2PQA · UniProt P15927 · UniProt P35244
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