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Peptidase module of the peptidoglycan hydrolase ripa (RV1477) from mycobacterium tuberculosis, catalytic site mutant (CYS383ALA) at 1.45 resolution
Analyse Peptidase module of the peptidoglycan hydrolase ripa (RV1477) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S0Q
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Invasion protein
- UniProt
- O53168
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Invasion protein | protein | 208 | 27% helix, 24% strand | O53168 |
Compared structures
- 3S0Q · Peptidase module of the peptidoglycan hydrolase RipA (Rv1477) from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00
- O53168 · AlphaFold monomer V2.0 prediction for peptidoglycan endopeptidase ripa (O53168) · 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 O53168
- Elsewhere: RCSB PDB 3S0Q · PDBe 3S0Q · UniProt O53168
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