Research workbench
Crystal structure of putative aminotransferase (mocr family) (YP_604413.1) from deinococcus geothermalis dsm 11300 at 2.60 a resolution
Analyse Crystal structure of putative aminotransferase (mocr family) (YP_604413.1) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EZ1
- Type
- protein
- Length
- 837 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aminotransferase mocr family
- UniProt
- Q1IZU0
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aminotransferase mocr family | protein | 418 | 44% helix, 15% strand | Q1IZU0 |
| B | Aminotransferase mocr family | protein | 419 | 43% helix, 15% strand | Q1IZU0 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.72 | 0.95 | 22 | PO4 |
| 2 | 237 | 0.71 | 0.87 | 38 | PO4 |
| 3 | 106 | 0.45 | 0.79 | 19 | empty |
| 4 | 63 | 0.39 | 0.80 | 14 | empty |
| 5 | 52 | 0.35 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2392 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3EZ1 · Crystal structure of putative aminotransferase (MocR family) (YP_604413.1) 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 Q1IZU0
- Elsewhere: RCSB PDB 3EZ1 · PDBe 3EZ1 · UniProt Q1IZU0
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