MolNFT v1 · #42087 · protein
Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form
2K7V · Dihydrolipoyllysine-residue acetyltransferase component of…: “Deletions in a surface loop divert the folding of a protein domain into a metastable dimeric form”. Solution nmr. MolNFT v1 #42087 on GenesisL1: 3D structure, binding…
- PDB
- 2K7V
- Type
- protein
- Length
- 170 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- EC
- 2.3.1.12
- UniProt
- P06959
Structure
solution nmr · 1 distinct chain · 0% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) | protein | 85 | 0% helix, 18% strand | P06959 |
Interfaces
1 interface between chains.
- A–B · 1609 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2K7V · Deletions in a surface loop divert the folding of a protein domain into a metastable… · the same entry in another collection · chain A against A, TM-score 1.00
- P06959 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.39
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 P06959
- Elsewhere: RCSB PDB 2K7V · PDBe 2K7V · UniProt P06959
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