Research workbench
Structural basis for the feedback regulation of escherichia COLI pantothenate kinase by coenzyme a
Analyse Structural basis for the feedback regulation of escherichia COLI pantothenate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ESN
- Type
- protein
- Length
- 1,238 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0A6I3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 311 | — | P0A6I3 |
| B, C, D | — | protein | 309 | — | P0A6I3 |
Compared structures
- 1ESN · Structural basis for the feedback regulation of escherichia COLI pantothenate kinase by… · the same entry in another collection · chain D against D, TM-score 1.00
- P0A6I3 · AlphaFold monomer V2.0 prediction for pantothenate kinase (P0A6I3) · a predicted model of the same protein · chain D 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 P0A6I3
- Elsewhere: RCSB PDB 1ESN · PDBe 1ESN · UniProt P0A6I3
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