Research workbench
X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp
Analyse X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q5J
- Type
- protein
- Length
- 1,053 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P51852
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 523 | — | P51852 |
| B | — | protein | 530 | — | P51852 |
Compared structures
- 2Q5J · X-ray structure of phenylpyruvate decarboxylase in complex with 3-deaza-ThDP · the same entry in another collection · chain A against A, TM-score 1.00
- P51852 · AlphaFold monomer V2.0 prediction for indole-3-pyruvate decarboxylase (P51852) · a predicted model of the same protein · 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 P51852
- Elsewhere: RCSB PDB 2Q5J · PDBe 2Q5J · UniProt P51852
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