MolNFT v1 · #31766 · protein
Wild type ssat- 1.7A structure
2B5G · Diamine acetyltransferase 1: “Wild type ssat- 1.7A structure”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.81). MolNFT v1 #31766 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2B5G
- Type
- protein
- Length
- 324 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
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diamine acetyltransferase 1 (EC 2.3.1.57) | protein | 164 | 40% helix, 30% strand | P21673 |
| B | Diamine acetyltransferase 1 | protein | 160 | 43% helix, 31% strand | P21673 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
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 | 992 | 0.81 | 0.82 | 97 | SO4 |
| 2 | 128 | 0.46 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 3525 Ų buried · 51 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified, 2 disulfide (engineered, disulfide, acetylation).
Compared structures
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 2B5G · PDBe 2B5G · UniProt P21673
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