Research workbench
Product peptide-bound structure of metalloprotease ZMP1 variant E143A from clostridium difficile
Analyse Product peptide-bound structure of metalloprotease ZMP1 variant E143A from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A0R
- Type
- protein
- Length
- 392 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q183R7
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 192 | — | Q183R7 |
| D, E | — | protein | 4 | — | — |
Compared structures
- 5A0R · Product peptide-bound structure of metalloprotease Zmp1 variant E143A from Clostridium… · the same entry in another collection · chain A against A, TM-score 1.00
- Q183R7 · AlphaFold monomer V2.0 prediction for pro-pro endopeptidase (Q183R7) · 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 Q183R7
- Elsewhere: RCSB PDB 5A0R · PDBe 5A0R · UniProt Q183R7
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