Research workbench
Structure of the mtr complex
Analyse Structure of the mtr complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R2Q
- Type
- protein
- Length
- 1,522 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystathionine beta-synthase; Uncharacterized protein; Decaheme C-type cytochrome…
- UniProt
- A0A165K349, A0A165K351, A0A379ZX38
- Ligands
- HEC, CA
- Pockets
- 18 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystathionine beta-synthase | protein | 265 | 28% helix, 5% strand | A0A165K349 |
| B | Uncharacterized protein | protein | 649 | 2% helix, 65% strand | A0A165K351 |
| C | Decaheme C-type cytochrome, OMCA/MTRC family | protein | 608 | 23% helix, 27% strand | A0A379ZX38 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 985 | 0.87 | 0.89 | 125 | HEC |
| 2 | 1107 | 0.85 | 0.85 | 133 | HEC |
| 3 | 379 | 0.84 | 0.93 | 60 | HEC |
| 4 | 631 | 0.81 | 0.85 | 55 | HEC |
| 5 | 258 | 0.80 | 0.92 | 65 | HEC |
Interfaces
3 interfaces between chains.
- A–B · 6189 Ų buried · 82 hydrogen bonds · protein-protein
- B–C · 832 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 546 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 cofactor, 2 disulfide (heme c attachment, disulfide).
Compared structures
- 6R2Q · Structure of the Mtr complex · 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 A0A165K349
- Every structure of UniProt A0A165K351
- Every structure of UniProt A0A379ZX38
- Elsewhere: RCSB PDB 6R2Q · PDBe 6R2Q · UniProt A0A165K349 · UniProt A0A165K351 · UniProt A0A379ZX38
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