Research workbench
Crystal structure of aspartate aminotransferase (E.C. 2.6.1.1) (YP_194538.1) from lactobacillus acidophilus ncfm at 2.15 a resolution
Analyse Crystal structure of aspartate aminotransferase (E.C. 2.6.1.1) (YP_194538.1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F6T
- Type
- protein
- Length
- 1,032 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate aminotransferase
- EC
- 2.6.1.1
- UniProt
- Q5FIG7
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate aminotransferase (EC 2.6.1.1) | protein | 515 | 53% helix, 13% strand | Q5FIG7 |
| B | Aspartate aminotransferase (EC 2.6.1.1) | protein | 517 | 52% helix, 13% strand | Q5FIG7 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.70 | 0.79 | 59 | empty |
| 2 | 543 | 0.69 | 0.79 | 58 | empty |
| 3 | 528 | 0.69 | 0.79 | 43 | EDO |
| 4 | 504 | 0.68 | 0.78 | 43 | EDO |
| 5 | 269 | 0.63 | 0.81 | 35 | EDO |
Interfaces
1 interface between chains.
- A–B · 3933 Ų buried · 52 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered, cofactor).
Compared structures
- 3F6T · Crystal structure of aspartate aminotransferase (E.C. 2.6.1.1) (YP_194538.1) from… · 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 Q5FIG7
- Elsewhere: RCSB PDB 3F6T · PDBe 3F6T · UniProt Q5FIG7
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