Research workbench
Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ale-1
Analyse Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R77
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O05156
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 99 | — | O05156 |
| B | — | protein | 103 | — | O05156 |
Compared structures
- 1R77 · Crystal structure of the cell wall targeting domain of peptidylglycan hydrolase ALE-1 · the same entry in another collection · chain A against A, TM-score 1.00
- O05156 · AlphaFold monomer V2.0 prediction for glycyl-glycine endopeptidase ale-1 (O05156) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O05156
- Elsewhere: RCSB PDB 1R77 · PDBe 1R77 · UniProt O05156
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