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Crystal structure of a DUF72 family protein (TM1631) from thermotoga maritima MSB8 at 2.20 a resolution
Analyse Crystal structure of a DUF72 family protein (TM1631) from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VPQ
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein TM1631
- UniProt
- Q9X1W6
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein TM1631 | protein | 260 | 40% helix, 19% strand | Q9X1W6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.55 | 0.79 | 25 | SO4 |
| 2 | 144 | 0.43 | 0.75 | 22 | empty |
Compared structures
- 1VPQ · CRYSTAL STRUCTURE OF a DUF72 family protein (TM1631) FROM THERMOTOGA MARITIMA MSB8 AT… · 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 Q9X1W6
- Elsewhere: RCSB PDB 1VPQ · PDBe 1VPQ · UniProt Q9X1W6
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