MolNFT v1 · #162808 · protein
Inter-dimeric interface controls function and stability of S- methionine adenosyltransferase from U. urealiticum
6RJS: “Inter-dimeric interface controls function and stability of S- methionine adenosyltransferase from U.…”. X-ray diffraction, 20 pockets (best druggability 0.73). MolNFT v1 #162808 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6RJS
- Type
- protein
- Length
- 1,440 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methionine adenosyltransferase
- EC
- 2.5.1.6
- UniProt
- B2NE58
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine adenosyltransferase (EC 2.5.1.6) | protein | 361 | 33% helix, 23% strand | B2NE58 |
| C | Methionine adenosyltransferase (EC 2.5.1.6) | protein | 358 | 33% helix, 24% strand | B2NE58 |
| B | Methionine adenosyltransferase (EC 2.5.1.6) | protein | 360 | 33% helix, 24% strand | B2NE58 |
| D | Methionine adenosyltransferase (EC 2.5.1.6) | protein | 361 | 33% helix, 23% strand | B2NE58 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.73 | 0.81 | 60 | empty |
| 2 | 649 | 0.73 | 0.80 | 65 | empty |
| 3 | 529 | 0.71 | 0.80 | 51 | empty |
| 4 | 484 | 0.70 | 0.80 | 47 | empty |
| 5 | 468 | 0.69 | 0.80 | 49 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2447 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 2432 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 337 Ų buried · 0 hydrogen bonds · protein-protein
- C–B · 331 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 328 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6RJS · Inter-dimeric interface controls function and stability of S-methionine… · 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 B2NE58
- Elsewhere: RCSB PDB 6RJS · PDBe 6RJS · UniProt B2NE58
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