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Crystal structure of tehb-like SAM-dependent methyltransferase (NP_600671.1) from corynebacterium glutamicum atcc 13032 kitasato at 2.00 a resolution
Analyse Crystal structure of tehb-like SAM-dependent methyltransferase (NP_600671.1)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CGG
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SAM-dependent methyltransferase
- UniProt
- Q6M5C6
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SAM-dependent methyltransferase | protein | 186 | 37% helix, 26% strand | Q6M5C6 |
| B | SAM-dependent methyltransferase | protein | 184 | 39% helix, 27% strand | Q6M5C6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A
- CIT · Citric acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.71 | 0.82 | 47 | NHE, EDO |
| 2 | 61 | 0.37 | 0.78 | 10 | empty |
| 3 | 61 | 0.29 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 791 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3CGG · Crystal structure of TehB-like SAM-dependent methyltransferase (NP_600671.1) 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 Q6M5C6
- Elsewhere: RCSB PDB 3CGG · PDBe 3CGG · UniProt Q6M5C6
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