Research workbench
Three tetrameric rings of isoaspartyl dipeptidase fitted in an EM volume.
Analyse Three tetrameric rings of isoaspartyl dipeptidase fitted in an EM volume. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LP3
- Type
- protein
- Length
- 4,508 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39377
Structure
electron microscopy · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, C, D, E | — | protein | 374 | — | P39377 |
| A, F, G, H | — | protein | 377 | — | P39377 |
| I, J, K, L | — | protein | 376 | — | P39377 |
Compared structures
- 5LP3 · Three tetrameric rings of Isoaspartyl Dipeptidase fitted in an EM volume. · the same entry in another collection · chain G against G, 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 P39377
- Elsewhere: RCSB PDB 5LP3 · PDBe 5LP3 · UniProt P39377
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