MolNFT v1 · #189747 · protein
Crystal structure of the core region of thermus thermophilus MUTS2.
7VUF · Endonuclease MUTS2: “Crystal structure of the core region of thermus thermophilus MUTS2.”. X-ray diffraction, 1 ligand (MG), 12 pockets (best druggability 0.71). MolNFT v1 #189747 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7VUF
- Type
- protein
- Length
- 1,869 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endonuclease MUTS2
- EC
- 3.1.-.-
- UniProt
- Q5SHT5
- Ligands
- MG
- Pockets
- 12 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Endonuclease MUTS2 (EC 3.1.-.-) | protein | 471 | 50% helix, 15% strand | Q5SHT5 |
| A | Endonuclease MUTS2 (EC 3.1.-.-) | protein | 462 | 49% helix, 12% strand | Q5SHT5 |
| C | Endonuclease MUTS2 (EC 3.1.-.-) | protein | 473 | 47% helix, 14% strand | Q5SHT5 |
| D | Endonuclease MUTS2 (EC 3.1.-.-) | protein | 463 | 49% helix, 12% strand | Q5SHT5 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains C
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains B, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 462 | 0.71 | 0.81 | 75 | PEG |
| 2 | 539 | 0.67 | 0.78 | 43 | empty |
| 3 | 189 | 0.61 | 0.82 | 32 | empty |
| 4 | 53 | 0.47 | 0.85 | 16 | empty |
| 5 | 50 | 0.45 | 0.85 | 15 | empty |
Interfaces
4 interfaces between chains.
- A–D · 1878 Ų buried · 15 hydrogen bonds · protein-protein
- B–A · 416 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 149 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 70 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 Q5SHT5
- Elsewhere: RCSB PDB 7VUF · PDBe 7VUF · UniProt Q5SHT5
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