MolNFT v1 · #35500 · protein
Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions: studies with halide compounds reveal a halide binding site in the active site
2EDA: “Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions…”. X-ray diffraction. MolNFT v1 #35500 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2EDA
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22643
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 310 | — | P22643 |
Compared structures
- 2EDA · Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase… · the same entry in another collection · chain A against A, TM-score 1.00
- P22643 · AlphaFold monomer V2.0 prediction for haloalkane dehalogenase (P22643) · 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 P22643
- Elsewhere: RCSB PDB 2EDA · PDBe 2EDA · UniProt P22643
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