Research workbench
Crystal structure of escherichia COLI holo-[acyl-carrier-protein] synthase (acps)
Analyse Crystal structure of escherichia COLI holo-[acyl-carrier-protein] synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XU7
- Type
- protein
- Length
- 358 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Holo-[acyl-carrier-protein] synthase
- EC
- 2.7.8.7
- UniProt
- P24224
- Ligands
- CL
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) | protein | 120 | 48% helix, 31% strand | P24224 |
| B, C | Holo-[acyl-carrier-protein] synthase (EC 2.7.8.7) | protein | 119 | 48% helix, 31% strand | P24224 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 220 | 0.53 | 0.77 | 37 | empty |
| 2 | 213 | 0.52 | 0.77 | 32 | empty |
| 3 | 77 | 0.33 | 0.74 | 21 | empty |
Interfaces
3 interfaces between chains.
- B–C · 686 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 685 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 679 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5XU7 · Crystal structure of Escherichia coli holo-[acyl-carrier-protein] synthase (AcpS) · the same entry in another collection · chain A against A, TM-score 1.00
- P24224 · AlphaFold monomer V2.0 prediction for holo-[acyl-carrier-protein] synthase (P24224) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P24224
- Elsewhere: RCSB PDB 5XU7 · PDBe 5XU7 · UniProt P24224
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.