Research workbench
The crystal structure of apo wild type cap at 3.6 a resolution.
Analyse The crystal structure of apo wild type cap at 3.6 a resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HIF
- Type
- protein
- Length
- 1,194 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ACK1
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 199 | — | P0ACK1 |
Compared structures
- 3HIF · The crystal structure of apo wild type CAP at 3.6 A resolution. · the same entry in another collection · chain F against F, TM-score 1.00
- P0ACK1 · AlphaFold monomer V2.0 prediction for camp-activated global transcriptional regulator crp… · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P0ACK1
- Elsewhere: RCSB PDB 3HIF · PDBe 3HIF · UniProt P0ACK1
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