Research workbench
Crystal structure of a putative nucleotidyltransferase (TM1012) from thermotoga maritima at 1.35 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
- 2FCL
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM1012
- Ligands
- UNL
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TM1012 | protein | 157 | 40% helix, 34% strand | — |
Ligands and binding sites
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 | 194 | 0.59 | 0.81 | 33 | empty |
| 2 | 54 | 0.27 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 15 modified (methylation).
Compared structures
- 2FCL · 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
- Elsewhere: RCSB PDB 2FCL · PDBe 2FCL
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