Research workbench
NMR structure of the catalytic domain from E. faecium L,D- transpeptidase
Analyse NMR structure of the catalytic domain from E. faecium L,D- transpeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZG4
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ERFK/YBIS/YCFS/YNHG
- EC
- 2.3.2.12
- UniProt
- Q3Y185
Structure
solution nmr · 1 distinct chain · 9% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ERFK/YBIS/YCFS/YNHG (EC 2.3.2.12) | protein | 129 | 9% helix, 36% strand | Q3Y185 |
Compared structures
- 3ZG4 · NMR structure of the catalytic domain from E. faecium L,D- transpeptidase · 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 Q3Y185
- Elsewhere: RCSB PDB 3ZG4 · PDBe 3ZG4 · UniProt Q3Y185
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