MolNFT v1 · #74558 · protein
Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed
3P0B · TT1467 protein: “Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action and products formed”. X-ray diffraction, 2 pockets (best druggability 0.72). MolNFT v1 #74558 on GenesisL1: 3D structure…
- PDB
- 3P0B
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TT1467 protein
- UniProt
- P84162
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TT1467 protein | protein | 511 | 52% helix, 13% strand | P84162 |
Ligands and binding sites
- GOL · Glycerol · 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 | 691 | 0.72 | 0.78 | 64 | empty |
| 2 | 121 | 0.44 | 0.77 | 19 | empty |
Compared structures
- 3P0B · Thermus thermophilus family GH57 branching enzyme: crystal structure, mechanism of action… · 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 P84162
- Elsewhere: RCSB PDB 3P0B · PDBe 3P0B · UniProt P84162
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