Research workbench
Conformational analysis of strh, the surface-attached exo- beta-D-N- acetylglucosaminidase from streptococcus pneumoniae
Analyse Conformational analysis of strh, the surface-attached exo- beta-D-N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LTJ
- Type
- protein
- Length
- 111 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-N-acetylhexosaminidase
- EC
- 3.2.1.52
- UniProt
- P49610
Structure
solution nmr · 1 distinct chain · 0% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-N-acetylhexosaminidase (EC 3.2.1.52) | protein | 111 | 0% helix, 32% strand | P49610 |
Compared structures
- 2LTJ · Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase… · the same entry in another collection · chain A against A, TM-score 1.00
- P49610 · AlphaFold monomer V2.0 prediction for beta-N-acetylhexosaminidase (P49610) · a predicted model of the same protein · chain A against A, TM-score 0.52
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 P49610
- Elsewhere: RCSB PDB 2LTJ · PDBe 2LTJ · UniProt P49610
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