MolNFT v1 · #1571 · protein
Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus stearothermophilus
1B5S: “Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus…”. X-ray diffraction. MolNFT v1 #1571 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1B5S
- Type
- protein
- Length
- 1,210 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11961
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | — | protein | 242 | — | P11961 |
Compared structures
- 1B5S · Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from… · the same entry in another collection · chain A against A, TM-score 1.00
- P11961 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P11961
- Elsewhere: RCSB PDB 1B5S · PDBe 1B5S · UniProt P11961
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