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Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine
Analyse Crystal structure of feedback inhibition resistant mutant of aspartate kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AB4
- Type
- protein
- Length
- 4,134 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartokinase
- EC
- 2.7.2.4
- UniProt
- P26512
- Ligands
- THR, LYS
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 16 distinct chains · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartokinase (EC 2.7.2.4) | protein | 370 | 41% helix, 24% strand | P26512 |
| B | Aspartokinase (EC 2.7.2.4) | protein | 157 | 32% helix, 35% strand | P26512 |
| C | Aspartokinase (EC 2.7.2.4) | protein | 367 | 42% helix, 26% strand | P26512 |
| D | Aspartokinase (EC 2.7.2.4) | protein | 150 | 35% helix, 37% strand | P26512 |
| E | Aspartokinase (EC 2.7.2.4) | protein | 368 | 40% helix, 25% strand | P26512 |
| F | Aspartokinase (EC 2.7.2.4) | protein | 148 | 32% helix, 39% strand | P26512 |
| G | Aspartokinase (EC 2.7.2.4) | protein | 357 | 40% helix, 27% strand | P26512 |
| H | Aspartokinase (EC 2.7.2.4) | protein | 151 | 29% helix, 33% strand | P26512 |
| I | Aspartokinase (EC 2.7.2.4) | protein | 360 | 42% helix, 26% strand | P26512 |
| J | Aspartokinase (EC 2.7.2.4) | protein | 132 | 37% helix, 36% strand | P26512 |
| K | Aspartokinase (EC 2.7.2.4) | protein | 373 | 40% helix, 25% strand | P26512 |
| L | Aspartokinase (EC 2.7.2.4) | protein | 156 | 35% helix, 37% strand | P26512 |
| M | Aspartokinase (EC 2.7.2.4) | protein | 377 | 41% helix, 25% strand | P26512 |
| N | Aspartokinase (EC 2.7.2.4) | protein | 155 | 34% helix, 35% strand | P26512 |
| O | Aspartokinase (EC 2.7.2.4) | protein | 364 | 41% helix, 24% strand | P26512 |
| P | Aspartokinase (EC 2.7.2.4) | protein | 149 | 33% helix, 35% strand | P26512 |
Ligands and binding sites
- THR · Threonine · ligand · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
- LYS · Lysine · ligand · 7 copies · chains A, B, C, D, E, F, G, H, K, L, M, N, O, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.77 | 0.82 | 73 | empty |
| 2 | 662 | 0.73 | 0.80 | 54 | empty |
| 3 | 560 | 0.72 | 0.80 | 52 | empty |
| 4 | 442 | 0.71 | 0.82 | 66 | empty |
| 5 | 515 | 0.71 | 0.81 | 49 | empty |
Interfaces
32 interfaces between chains.
- K–L · 2780 Ų buried · 44 hydrogen bonds · protein-protein
- M–N · 2720 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 2455 Ų buried · 36 hydrogen bonds · protein-protein
- E–F · 2442 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 2398 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 3AB4 · Crystal structure of feedback inhibition resistant mutant of aspartate kinase from… · the same entry in another collection · chain C against C, 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 P26512
- Elsewhere: RCSB PDB 3AB4 · PDBe 3AB4 · UniProt P26512
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