Research workbench
Crystal structure of a C-C bond hydrolase, bphd, from burkholderia xenovorans LB400
Analyse Crystal structure of a C-C bond hydrolase, bphd, from burkholderia xenovorans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PU5
- Type
- protein
- Length
- 568 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P47229
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 285 | — | P47229 |
| B | — | protein | 283 | — | P47229 |
Compared structures
- 2PU5 · Crystal Structure of a C-C bond hydrolase, BphD, from Burkholderia xenovorans LB400 · the same entry in another collection · chain A against A, TM-score 1.00
- P47229 · AlphaFold monomer V2.0 prediction for 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase… · a predicted model of the same protein · chain A 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 P47229
- Elsewhere: RCSB PDB 2PU5 · PDBe 2PU5 · UniProt P47229
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