Research workbench
Crystal structure of P-cresol methylhydroxylase at 2.5 a resolution
Analyse Crystal structure of P-cresol methylhydroxylase at 2.5 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DII
- Type
- protein
- Length
- 1,176 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09788, P09787
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 515 | — | P09788 |
| C, D | — | protein | 73 | — | P09787 |
Compared structures
- 1DII · Crystal structure of P-cresol methylhydroxylase at 2.5 a resolution · the same entry in another collection · chain D against D, TM-score 1.00
- P09788 · AlphaFold monomer V2.0 prediction for 4-cresol dehydrogenase [hydroxylating] flavoprotein… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P09787 · AlphaFold monomer V2.0 prediction for 4-cresol dehydrogenase [hydroxylating] cytochrome C… · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P09788
- Every structure of UniProt P09787
- Elsewhere: RCSB PDB 1DII · PDBe 1DII · UniProt P09788 · UniProt P09787
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