Research workbench
Crystal structure of B. subtilis maf protein complexed with D-(UTP)
Analyse Crystal structure of B. subtilis maf protein complexed with D-(UTP) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EXC
- Type
- protein
- Length
- 370 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein maf
- UniProt
- Q02169
- Ligands
- DUT, NA
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein maf | protein | 185 | 36% helix, 26% strand | Q02169 |
Ligands and binding sites
- DUT · Deoxyuridine-5'-triphosphate · ligand · 4 copies · chains A, B
- NA · Sodium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 441 | 0.63 | 0.77 | 49 | DUT |
| 2 | 308 | 0.63 | 0.80 | 42 | DUT |
| 3 | 305 | 0.61 | 0.79 | 42 | DUT |
| 4 | 81 | 0.43 | 0.79 | 17 | empty |
| 5 | 69 | 0.32 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 594 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1EXC · Crystal structure of B. subtilis maf protein complexed with D-(UTP) · the same entry in another collection · chain A against A, TM-score 1.00
- Q02169 · AlphaFold monomer V2.0 prediction for DTTP/UTP pyrophosphatase (Q02169) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q02169
- Elsewhere: RCSB PDB 1EXC · PDBe 1EXC · UniProt Q02169
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