MolNFT v1 · #172433 · protein
Structure-function analyses of dual-bon domain protein dolp identifies phospholipid binding as a new mechanism for protein localisation to the cell division site
7A2D: “Structure-function analyses of dual-bon domain protein dolp identifies phospholipid binding as a new…”. Solution nmr. MolNFT v1 #172433 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7A2D
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P64596
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 178 | — | P64596 |
Compared structures
- 7A2D · Structure-function analyses of dual-BON domain protein DolP identifies phospholipid… · the same entry in another collection · chain A against A, TM-score 1.00
- P64596 · AlphaFold monomer V2.0 prediction for uncharacterized protein yrap (P64596) · a predicted model of the same protein · chain A against A, TM-score 0.46
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 P64596
- Elsewhere: RCSB PDB 7A2D · PDBe 7A2D · UniProt P64596
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