Research workbench
Structural characterization of a complex between the acidic transactivation domain of EBNA2 and the TFB1/P62 subunit of tfiih.
Analyse Structural characterization of a complex between the acidic transactivation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MKR
- Type
- protein
- Length
- 128 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P32776, P12978
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 115 | — | P32776 |
| B | — | protein | 13 | — | P12978 |
Compared structures
- 2MKR · Structural Characterization of a Complex Between the Acidic Transactivation Domain of… · the same entry in another collection · chain A against A, TM-score 1.00
- P32776 · AlphaFold monomer V2.0 prediction for general transcription and DNA repair factor iih… · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P32776
- Every structure of UniProt P12978
- Elsewhere: RCSB PDB 2MKR · PDBe 2MKR · UniProt P32776 · UniProt P12978
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