Research workbench
Inter-subunit signaling in gsam
Analyse Inter-subunit signaling in gsam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HOY
- Type
- protein
- Length
- 795 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamate-1-semialdehyde 2,1-aminomutase (gsam) apo-form
- EC
- 5.4.3.8
- UniProt
- P24630
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate-1-semialdehyde 2,1-aminomutase (gsam) apo-form (EC 5.4.3.8) | protein | 402 | 41% helix, 17% strand | P24630 |
| B | Glutamate-1-semialdehyde 2,1-aminomutase (gsam) apo-form (EC 5.4.3.8) | protein | 393 | 42% helix, 18% strand | P24630 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.76 | 1.00 | 18 | empty |
| 2 | 58 | 0.75 | 0.99 | 18 | empty |
| 3 | 744 | 0.72 | 0.78 | 65 | PO4 |
| 4 | 283 | 0.72 | 0.86 | 45 | PO4 |
| 5 | 100 | 0.46 | 0.80 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3732 Ų buried · 49 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 P24630
- Elsewhere: RCSB PDB 2HOY · PDBe 2HOY · UniProt P24630
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