MolNFT v1 · #188251 · protein
Structure of the S. aureus amidase lyth and activator acth extracellular domains
7TJ4: “Structure of the S. aureus amidase lyth and activator acth extracellular domains”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #188251 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7TJ4
- Type
- protein
- Length
- 595 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2X3YEX3, O32421
- Ligands
- ZN
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 122 | — | A0A2X3YEX3 |
| B | — | protein | 176 | — | O32421 |
| D | — | protein | 175 | — | O32421 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7TJ4 · Structure of the S. aureus amidase LytH and activator ActH extracellular domains · the same entry in another collection · chain A against A, TM-score 1.00
- O32421 · AlphaFold monomer V2.0 prediction for probable cell wall amidase lyth (O32421) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 A0A2X3YEX3
- Every structure of UniProt O32421
- Elsewhere: RCSB PDB 7TJ4 · PDBe 7TJ4 · UniProt A0A2X3YEX3 · UniProt O32421
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