Research workbench
Crystal structure of M-pmv dutpase relaxed end-product (dump) complex
Analyse Crystal structure of M-pmv dutpase relaxed end-product (dump) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TTA
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyuridine 5'-triphosphate nucleotido hydrolase
- EC
- 3.6.1.23
- UniProt
- O92810
- Ligands
- UMP
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyuridine 5'-triphosphate nucleotido hydrolase (EC 3.6.1.23) | protein | 113 | 10% helix, 40% strand | O92810 |
Ligands and binding sites
- UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3TTA · Crystal structure of M-PMV DUTPASE relaxed end-product (dUMP) 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 O92810
- Elsewhere: RCSB PDB 3TTA · PDBe 3TTA · UniProt O92810
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