Research workbench
Catalytic amidase domain of the major autolysin lyta from streptococcus pneumaniae
Analyse Catalytic amidase domain of the major autolysin lyta from streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IVV
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Autolysin
- EC
- 3.5.1.28
- UniProt
- P06653
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Autolysin (EC 3.5.1.28) | protein | 174 | 36% helix, 16% strand | P06653 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.39 | 0.76 | 19 | empty |
Compared structures
- 4IVV · Catalytic amidase domain of the major autolysin LytA from Streptococcus pneumaniae · the same entry in another collection · chain A against A, TM-score 1.00
- P06653 · AlphaFold monomer V2.0 prediction for autolysin (P06653) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P06653
- Elsewhere: RCSB PDB 4IVV · PDBe 4IVV · UniProt P06653
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