Research workbench
Structure of the LYS9MET mutant of the E. COLI proline utilization a (puta) DNA-binding domain.
Analyse Structure of the LYS9MET mutant of the E. COLI proline utilization a (puta)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AY0
- Type
- protein
- Length
- 261 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional puta protein
- UniProt
- P09546
- Ligands
- CL
Structure
x-ray diffraction · 4 distinct chains · 67% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | Bifunctional puta protein | protein | 43 | 65% helix, 16% strand | P09546 |
| B | Bifunctional puta protein | protein | 42 | 64% helix, 17% strand | P09546 |
| C, E | Bifunctional puta protein | protein | 44 | 68% helix, 18% strand | P09546 |
| D | Bifunctional puta protein | protein | 45 | 69% helix, 18% strand | P09546 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
11 interfaces between chains.
- C–D · 1646 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1619 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1578 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 483 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 451 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2AY0 · Structure of the Lys9Met mutant of the E. coli Proline Utilization A (PutA) DNA-binding… · the same entry in another collection · chain F against F, TM-score 1.00
- P09546 · AlphaFold monomer V2.0 prediction for bifunctional protein puta (P09546) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 P09546
- Elsewhere: RCSB PDB 2AY0 · PDBe 2AY0 · UniProt P09546
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