MolNFT v1 · #68816 · protein
C-terminal (adenylylation) domain of E.COLI glutamine synthetase adenylyltransferase
3K7D · Glutamate-ammonia-ligase adenylyltransferase: “C-terminal (adenylylation) domain of E.COLI glutamine synthetase adenylyltransferase”. X-ray diffraction, 1 ligand (SO4), 15 pockets (best druggability 0.74). MolNFT v1 #68816 on…
- PDB
- 3K7D
- Type
- protein
- Length
- 992 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate-ammonia-ligase adenylyltransferase
- EC
- 2.7.7.42
- UniProt
- P30870
- Ligands
- SO4
- Pockets
- 15 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate-ammonia-ligase adenylyltransferase (EC 2.7.7.42) | protein | 497 | 64% helix, 7% strand | P30870 |
| B | Glutamate-ammonia-ligase adenylyltransferase (EC 2.7.7.42) | protein | 495 | 63% helix, 7% strand | P30870 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 612 | 0.74 | 0.81 | 63 | SO4 |
| 2 | 631 | 0.72 | 0.80 | 62 | SO4 |
| 3 | 103 | 0.52 | 0.82 | 25 | empty |
| 4 | 171 | 0.51 | 0.78 | 31 | empty |
| 5 | 117 | 0.49 | 0.80 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1654 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3K7D · C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- P30870 · AlphaFold monomer V2.0 prediction for bifunctional glutamine synthetase… · a predicted model of the same protein · 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 P30870
- Elsewhere: RCSB PDB 3K7D · PDBe 3K7D · UniProt P30870
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