MolNFT v1 · #36433 · protein
X-ray structure of SPERMIDINE/SPERMINE N1-acetyltransferase (sat) from homo sapiens
2F5I · Diamine acetyltransferase 1: “X-ray structure of SPERMIDINE/SPERMINE N1-acetyltransferase (sat) from homo sapiens”. X-ray diffraction, 2 pockets (best druggability 0.82). MolNFT v1 #36433 on GenesisL1: 3D structure, binding sites…
- PDB
- 2F5I
- Type
- protein
- Length
- 335 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diamine acetyltransferase 1
- EC
- 2.3.1.57
- UniProt
- P21673
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diamine acetyltransferase 1 (EC 2.3.1.57) | protein | 167 | 39% helix, 29% strand | P21673 |
| B | Diamine acetyltransferase 1 (EC 2.3.1.57) | protein | 168 | 39% helix, 29% strand | P21673 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 998 | 0.82 | 0.83 | 102 | empty |
| 2 | 59 | 0.52 | 0.86 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3767 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 2F5I · X-ray structure of spermidine/spermine N1-acetyltransferase (SAT) from Homo sapiens · the same entry in another collection · chain A against A, TM-score 1.00
- P21673 · AlphaFold monomer V2.0 prediction for diamine acetyltransferase 1 (P21673) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P21673
- Elsewhere: RCSB PDB 2F5I · PDBe 2F5I · UniProt P21673
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