MolNFT v1 · #48259 · protein
Crystal structure of the asymmetric PDK3-L2 complex
2PNR: “Crystal structure of the asymmetric PDK3-L2 complex”. X-ray diffraction. MolNFT v1 #48259 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PNR
- Type
- protein
- Length
- 1,588 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15120, P10515
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 374 | — | Q15120 |
| B, F | — | protein | 341 | — | Q15120 |
| C, G | — | protein | 79 | — | P10515 |
Compared structures
- 2PNR · Crystal Structure of the asymmetric Pdk3-l2 Complex · the same entry in another collection · chain G against G, TM-score 1.00
- Q15120 · AlphaFold monomer V2.0 prediction for [pyruvate dehydrogenase (acetyl-transferring)]… · a predicted model of the same protein · chain B against A, TM-score 0.98
- P10515 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain C 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 Q15120
- Every structure of UniProt P10515
- Elsewhere: RCSB PDB 2PNR · PDBe 2PNR · UniProt Q15120 · UniProt P10515
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