Research workbench
Escherichia COLI agpase mutant R130A apo form
Analyse Escherichia COLI agpase mutant R130A apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MNI
- Type
- protein
- Length
- 3,182 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucose-1-phosphate adenylyltransferase
- EC
- 2.7.7.27
- UniProt
- P0A6V1
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 8 distinct chains · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 401 | 27% helix, 30% strand | P0A6V1 |
| G | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 393 | 29% helix, 28% strand | P0A6V1 |
| H | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 393 | 28% helix, 29% strand | P0A6V1 |
| F | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 390 | 29% helix, 30% strand | P0A6V1 |
| A | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 396 | 28% helix, 30% strand | P0A6V1 |
| B | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 406 | 28% helix, 29% strand | P0A6V1 |
| D | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 409 | 27% helix, 29% strand | P0A6V1 |
| C | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) | protein | 394 | 29% helix, 31% strand | P0A6V1 |
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 | 1167 | 0.89 | 0.90 | 133 | empty |
| 2 | 691 | 0.87 | 0.91 | 82 | empty |
| 3 | 286 | 0.82 | 0.93 | 51 | empty |
| 4 | 877 | 0.79 | 0.82 | 102 | empty |
| 5 | 933 | 0.79 | 0.81 | 100 | empty |
Interfaces
13 interfaces between chains.
- A–B · 1455 Ų buried · 31 hydrogen bonds · protein-protein
- D–C · 1454 Ų buried · 33 hydrogen bonds · protein-protein
- G–H · 1448 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 1443 Ų buried · 33 hydrogen bonds · protein-protein
- E–H · 985 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
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 P0A6V1
- Elsewhere: RCSB PDB 5MNI · PDBe 5MNI · UniProt P0A6V1
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