MolNFT v1 · #40772 · protein
Dimerization is important for the GTPase activity of chloroplast translocon components ATTOC33 and PSTOC159
2J3E: “Dimerization is important for the GTPase activity of chloroplast translocon components ATTOC33 and PSTOC159”. X-ray diffraction. MolNFT v1 #40772 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2J3E
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O23680
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 249 | — | O23680 |
Compared structures
- 2J3E · Dimerization is important for the GTPase activity of chloroplast translocon components… · the same entry in another collection · chain A against A, TM-score 1.00
- O23680 · AlphaFold monomer V2.0 prediction for translocase of chloroplast 33, chloroplastic… · 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 O23680
- Elsewhere: RCSB PDB 2J3E · PDBe 2J3E · UniProt O23680
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