Research workbench
C1A mutant of E. COLI glms in complex with glucose-6P and glutamate
Analyse C1A mutant of E. COLI glms in complex with glucose-6P and glutamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OOJ
- Type
- protein
- Length
- 4,828 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing
- UniProt
- C9QXA7
- Ligands
- GLU, G6Q, G6P
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 6 distinct chains · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, H | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 608 | 39% helix, 22% strand | C9QXA7 |
| C | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 601 | 39% helix, 21% strand | C9QXA7 |
| D | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 602 | 39% helix, 22% strand | C9QXA7 |
| E | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 602 | 39% helix, 22% strand | C9QXA7 |
| F | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 594 | 39% helix, 21% strand | C9QXA7 |
| G | GLUCOSAMINE/FRUCTOSE-6-phosphate aminotransferase, isomerizing | protein | 605 | 40% helix, 23% strand | C9QXA7 |
Ligands and binding sites
- GLU · Glutamic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- G6Q · Glucose-6-phosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- G6P · 6-O-phosphono-alpha-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H
- GOL · Glycerol · additive · 8 copies · chains A, B, C, D, E, F, G, H
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 | 700 | 0.88 | 0.92 | 58 | empty |
| 2 | 589 | 0.87 | 0.92 | 65 | empty |
| 3 | 571 | 0.87 | 0.92 | 61 | empty |
| 4 | 583 | 0.87 | 0.92 | 69 | empty |
| 5 | 881 | 0.80 | 0.82 | 73 | empty |
Interfaces
15 interfaces between chains.
- E–F · 2697 Ų buried · 50 hydrogen bonds · protein-protein
- A–B · 2684 Ų buried · 55 hydrogen bonds · protein-protein
- C–D · 2681 Ų buried · 51 hydrogen bonds · protein-protein
- G–H · 2627 Ų buried · 45 hydrogen bonds · protein-protein
- B–H · 1538 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 3OOJ · C1A mutant of E. coli GlmS in complex with glucose-6P and glutamate · 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 C9QXA7
- Elsewhere: RCSB PDB 3OOJ · PDBe 3OOJ · UniProt C9QXA7
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