Research workbench
Crystal structure of P1G mutant of D-dopachrome tautomerase
Analyse Crystal structure of P1G mutant of D-dopachrome tautomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MW7
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-dopachrome decarboxylase
- EC
- 4.1.1.84
- UniProt
- P30046
- Ligands
- NA, SO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-dopachrome decarboxylase (EC 4.1.1.84) | protein | 118 | 40% helix, 30% strand | P30046 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P30046
- Elsewhere: RCSB PDB 7MW7 · PDBe 7MW7 · UniProt P30046
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