Research workbench
TEG12 APO
Analyse TEG12 APO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MGC
- Type
- protein
- Length
- 482 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TEG12
- EC
- 2.8.2.-
- UniProt
- B7T1D7
- Ligands
- PME
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TEG12 (EC 2.8.2.-) | protein | 255 | 45% helix, 11% strand | B7T1D7 |
| B | TEG12 (EC 2.8.2.-) | protein | 227 | 50% helix, 12% strand | B7T1D7 |
Ligands and binding sites
- PME · N-L-alpha-aspartyl L-phenylalanine 1-methyl ester · ligand · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.58 | 0.76 | 38 | PME |
| 2 | 239 | 0.48 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 610 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3MGC · Teg12 Apo · 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 B7T1D7
- Elsewhere: RCSB PDB 3MGC · PDBe 3MGC · UniProt B7T1D7
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