Research workbench
Crystal structure of a putative nucleotidyltransferase (TM1012) from thermotoga maritima at 1.60 a resolution
Analyse Crystal structure of a putative nucleotidyltransferase (TM1012) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EWR
- Type
- protein
- Length
- 156 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM1012
- UniProt
- Q9X0A5
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TM1012 | protein | 156 | 40% helix, 34% strand | Q9X0A5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
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 | 259 | 0.62 | 0.81 | 38 | EDO |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2EWR · Crystal structure of a putative nucleotidyltransferase (tm1012) from Thermotoga maritima… · 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 Q9X0A5
- Elsewhere: RCSB PDB 2EWR · PDBe 2EWR · UniProt Q9X0A5
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