Research workbench
Crystal structure of ethanolamine ammonia-lyase from escherichia COLI complexed with cn-cbl and ethanolamine
Analyse Crystal structure of ethanolamine ammonia-lyase from escherichia COLI complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ABO
- Type
- protein
- Length
- 1,406 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AEJ6, P19636
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 453 | — | P0AEJ6 |
| B | — | protein | 252 | — | P19636 |
| D | — | protein | 248 | — | P19636 |
Compared structures
- 3ABO · Crystal structure of ethanolamine ammonia-lyase from Escherichia coli complexed with… · the same entry in another collection · chain D against D, TM-score 1.00
- P19636 · AlphaFold monomer V2.0 prediction for ethanolamine ammonia-lyase light chain (P19636) · a predicted model of the same protein · chain D against A, TM-score 1.00
- P0AEJ6 · AlphaFold monomer V2.0 prediction for ethanolamine ammonia-lyase heavy chain (P0AEJ6) · a predicted model of the same protein · chain C 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 P0AEJ6
- Every structure of UniProt P19636
- Elsewhere: RCSB PDB 3ABO · PDBe 3ABO · UniProt P0AEJ6 · UniProt P19636
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