Research workbench
Crystal structure of M-pmv dutpase complexed with dupnpp, substrate
Analyse Crystal structure of M-pmv dutpase complexed with dupnpp, substrate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TPN
- 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
- DUP, MG
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyuridine 5'-triphosphate nucleotido hydrolase (EC 3.6.1.23) | protein | 113 | 10% helix, 44% strand | O92810 |
Ligands and binding sites
- DUP · 2'-deoxyuridine 5'-alpha,beta-imido-triphosphate · ligand · chains A
- MG · Magnesium ion · metal
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (additive adduct).
Compared structures
- 3TPN · Crystal structure of M-PMV dUTPASE complexed with dUPNPP, substrate · 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 3TPN · PDBe 3TPN · UniProt O92810
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