Research workbench
Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii
Analyse Combined solid-state NMR, solution-state NMR and EM data for structure… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F3K
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- electron microscopy; solution nmr; solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrahedral aminopeptidase
- EC
- 3.4.11.-
- UniProt
- O59196
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.38
Structure
electron microscopy; solution nmr; solid-state nmr · 1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetrahedral aminopeptidase (EC 3.4.11.-) | protein | 353 | 29% helix, 20% strand | O59196 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.38 | 0.76 | 25 | empty |
| 2 | 62 | 0.35 | 0.77 | 15 | empty |
| 3 | 69 | 0.32 | 0.75 | 17 | empty |
| 4 | 57 | 0.28 | 0.74 | 16 | empty |
Compared structures
- 6F3K · Combined solid-state NMR, solution-state NMR and EM data for structure determination of… · the same entry in another collection · chain A against A, TM-score 1.00
- O59196 · AlphaFold monomer V2.0 prediction for tetrahedral aminopeptidase (O59196) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 O59196
- Elsewhere: RCSB PDB 6F3K · PDBe 6F3K · UniProt O59196
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