Research workbench
Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by tlck
Analyse Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NSY
- Type
- protein
- Length
- 531 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7M135
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 265 | — | Q7M135 |
| B | — | protein | 266 | — | Q7M135 |
Compared structures
- 4NSY · Wild-type lysobacter enzymogenes lysc endoproteinase covalently inhibited by TLCK · the same entry in another collection · chain B against B, TM-score 1.00
- Q7M135 · AlphaFold monomer V2.0 prediction for lysyl endopeptidase (Q7M135) · a predicted model of the same protein · chain B 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 Q7M135
- Elsewhere: RCSB PDB 4NSY · PDBe 4NSY · UniProt Q7M135
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