Research workbench
Crystal structure of thermus thermophilus TTHA1280, a putative SAM- dependent RNA methyltransferase, in complex with S-adenosyl-L- homocysteine
Analyse Crystal structure of thermus thermophilus TTHA1280, a putative SAM- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CWW
- Type
- protein
- Length
- 758 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative SAM-dependent RNA methyltransferase
- UniProt
- Q5SIT4
- Ligands
- SAH
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative SAM-dependent RNA methyltransferase | protein | 376 | 33% helix, 33% strand | Q5SIT4 |
| B | Putative SAM-dependent RNA methyltransferase | protein | 382 | 32% helix, 32% strand | Q5SIT4 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- ACY · Acetic acid · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1024 | 0.74 | 0.77 | 110 | SAH |
| 2 | 801 | 0.72 | 0.77 | 74 | SAH |
| 3 | 80 | 0.30 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 427 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2CWW · Crystal structure of Thermus thermophilus TTHA1280, a putative SAM-dependent RNA… · the same entry in another collection · chain B against B, 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 Q5SIT4
- Elsewhere: RCSB PDB 2CWW · PDBe 2CWW · UniProt Q5SIT4
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