MolNFT v1 · #61162 · protein
Crystal structure of a putative acetyltransferase (NP_142035.1) from pyrococcus horikoshii at 2.25 a resolution
3DDD: “Crystal structure of a putative acetyltransferase (NP_142035.1) from pyrococcus horikoshii at 2.25 a…”. X-ray diffraction, 1 ligand (COA), 1 pocket (best druggability 0.76). MolNFT v1 #61162 on GenesisL1: 3D structure, binding sites…
- PDB
- 3DDD
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative acetyltransferase
- UniProt
- O57768
- Ligands
- COA
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative acetyltransferase | protein | 281 | 36% helix, 31% strand | O57768 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 612 | 0.76 | 0.82 | 56 | COA |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3DDD · Crystal structure of A Putative Acetyltransferase (NP_142035.1) from PYROCOCCUS… · 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 O57768
- Elsewhere: RCSB PDB 3DDD · PDBe 3DDD · UniProt O57768
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