Research workbench
Crystal structure of the complex of phosphopantetheine adenylyltransferase from acinetobacter baumannii with citrate at 2.3 a resolution.
Analyse Crystal structure of the complex of phosphopantetheine adenylyltransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H16
- Type
- protein
- Length
- 972 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphopantetheine adenylyltransferase
- EC
- 2.7.7.3
- UniProt
- A0A059ZFC5
- Pockets
- 13 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, F | Phosphopantetheine adenylyltransferase (EC 2.7.7.3) | protein | 163 | 44% helix, 17% strand | A0A059ZFC5 |
| B, C, D | Phosphopantetheine adenylyltransferase (EC 2.7.7.3) | protein | 161 | 45% helix, 17% strand | A0A059ZFC5 |
Ligands and binding sites
- CIT · Citric acid · additive · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.82 | 0.83 | 107 | CIT |
| 2 | 730 | 0.80 | 0.84 | 85 | CIT |
| 3 | 142 | 0.79 | 0.96 | 22 | empty |
| 4 | 543 | 0.78 | 0.84 | 54 | CIT |
| 5 | 135 | 0.77 | 0.95 | 21 | empty |
Interfaces
15 interfaces between chains.
- A–F · 1213 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 1193 Ų buried · 12 hydrogen bonds · protein-protein
- B–E · 1191 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 698 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 678 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5H16 · Crystal structure of the complex of Phosphopantetheine adenylyltransferase from… · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A059ZFC5
- Elsewhere: RCSB PDB 5H16 · PDBe 5H16 · UniProt A0A059ZFC5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.