Research workbench
Crystal structure of the MTH889 protein from methanothermobacter thermautotrophicus. northeast structural genomics consortium target TT205
Analyse Crystal structure of the MTH889 protein from methanothermobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RAQ
- Type
- protein
- Length
- 652 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved protein MTH889
- UniProt
- O26975
- Ligands
- CA
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E, F, G | Conserved protein MTH889 | protein | 93 | 22% helix, 40% strand | O26975 |
| B | Conserved protein MTH889 | protein | 94 | 20% helix, 40% strand | O26975 |
Ligands and binding sites
- CA · Calcium ion · metal · 14 copies · chains A, B, G, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.34 | 0.77 | 13 | empty |
| 2 | 57 | 0.31 | 0.75 | 15 | empty |
Interfaces
14 interfaces between chains.
- C–D · 964 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 955 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 951 Ų buried · 11 hydrogen bonds · protein-protein
- A–G · 951 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 938 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2RAQ · Crystal structure of the MTH889 protein from Methanothermobacter thermautotrophicus.… · 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 O26975
- Elsewhere: RCSB PDB 2RAQ · PDBe 2RAQ · UniProt O26975
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