MolNFT v1 · #30588 · protein
Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by mineralocorticoid receptor
2A3I: “Structural and biochemical mechanisms for the specificity of hormone binding and coactivator assembly by…”. X-ray diffraction. MolNFT v1 #30588 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2A3I
- Type
- protein
- Length
- 265 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P08235, Q15788
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 253 | — | P08235 |
| B | — | protein | 12 | — | Q15788 |
Compared structures
- 2A3I · Structural and Biochemical Mechanisms for the Specificity of Hormone Binding and… · the same entry in another collection · chain A against A, TM-score 1.00
- P08235 · AlphaFold monomer V2.0 prediction for mineralocorticoid receptor (P08235) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P08235
- Every structure of UniProt Q15788
- Elsewhere: RCSB PDB 2A3I · PDBe 2A3I · UniProt P08235 · UniProt Q15788
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