MolNFT v1 · #57553 · protein
Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum in complex with lysine and threonine
3AB4 · Aspartokinase: “Crystal structure of feedback inhibition resistant mutant of aspartate kinase from corynebacterium glutamicum…”. X-ray diffraction, 2 ligands (THR, LYS), 20 pockets (best druggability 0.77). MolNFT v1 #57553 on…
- 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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