Research workbench
Crystal structure of putative phosphate acetyltransferase (NP_416953.1) from escherichia COLI K12 at 2.32 a resolution
Analyse Crystal structure of putative phosphate acetyltransferase (NP_416953.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VMI
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative phosphate acetyltransferase
- EC
- 2.3.1.8
- UniProt
- P77218
- Pockets
- 5 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative phosphate acetyltransferase (EC 2.3.1.8) | protein | 329 | 47% helix, 17% strand | P77218 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 209 | 0.54 | 0.78 | 29 | empty |
| 2 | 114 | 0.43 | 0.77 | 24 | empty |
| 3 | 80 | 0.33 | 0.74 | 15 | empty |
| 4 | 72 | 0.31 | 0.73 | 19 | empty |
| 5 | 53 | 0.29 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1VMI · Crystal structure of Putative phosphate acetyltransferase (np_416953.1) from Escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
- P77218 · AlphaFold monomer V2.0 prediction for ethanolamine utilization protein eutd (P77218) · a predicted model of the same protein · chain A 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 P77218
- Elsewhere: RCSB PDB 1VMI · PDBe 1VMI · UniProt P77218
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