MolNFT v1 · #57021 · protein
Crystal structure of putative acetyltransferase from T. thermophilus HB8
2ZXV · Putative uncharacterized protein TTHA1799: “Crystal structure of putative acetyltransferase from T. thermophilus HB8”. X-ray diffraction, 7 pockets (best druggability 0.79). MolNFT v1 #57021 on GenesisL1: 3D structure, binding sites…
- PDB
- 2ZXV
- Type
- protein
- Length
- 752 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein TTHA1799
- EC
- 2.3.1.128
- UniProt
- Q5SHD1
- Pockets
- 7 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative uncharacterized protein TTHA1799 (EC 2.3.1.128) | protein | 188 | 32% helix, 29% strand | Q5SHD1 |
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.79 | 0.82 | 95 | empty |
| 2 | 313 | 0.76 | 0.87 | 43 | empty |
| 3 | 158 | 0.74 | 0.92 | 31 | empty |
| 4 | 342 | 0.70 | 0.83 | 51 | empty |
| 5 | 484 | 0.64 | 0.77 | 46 | empty |
Interfaces
5 interfaces between chains.
- A–C · 1022 Ų buried · 25 hydrogen bonds · protein-protein
- B–D · 1002 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 439 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 433 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 303 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 2ZXV · Crystal structure of putative acetyltransferase from T. thermophilus HB8 · 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 Q5SHD1
- Elsewhere: RCSB PDB 2ZXV · PDBe 2ZXV · UniProt Q5SHD1
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