Research workbench
Crystal structure of the autolysin auto (LMO1076) from listeria monocytogenes, catalytic domain
Analyse Crystal structure of the autolysin auto (LMO1076) from listeria monocytogenes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FI7
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LMO1076 protein
- EC
- 3.2.1.96
- UniProt
- Q8Y842
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LMO1076 protein (EC 3.2.1.96) | protein | 177 | 46% helix, 14% strand | Q8Y842 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3FI7 · Crystal Structure of the autolysin Auto (Lmo1076) from Listeria monocytogenes, catalytic… · the same entry in another collection · 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 Q8Y842
- Elsewhere: RCSB PDB 3FI7 · PDBe 3FI7 · UniProt Q8Y842
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