Research workbench
Crystal structure of the conserved protein MTH1675 from methanobacterium thermoautotrophicum
Analyse Crystal structure of the conserved protein MTH1675 from methanobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T57
- Type
- protein
- Length
- 558 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved protein MTH1675
- UniProt
- O27711
- Ligands
- FMN, MG
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Conserved protein MTH1675 | protein | 186 | 40% helix, 22% strand | O27711 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 4 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.69 | 0.97 | 26 | empty |
| 2 | 227 | 0.65 | 0.83 | 36 | MG, FMN |
| 3 | 233 | 0.60 | 0.81 | 31 | FMN |
| 4 | 227 | 0.59 | 0.80 | 32 | FMN |
| 5 | 222 | 0.53 | 0.77 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1701 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 1537 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 211 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 modified (engineered).
Compared structures
- 1T57 · Crystal Structure of the Conserved Protein MTH1675 from Methanobacterium… · 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 O27711
- Elsewhere: RCSB PDB 1T57 · PDBe 1T57 · UniProt O27711
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