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The crystal structure of N-acetylmuramoyl-L-alanine amidase from clostridium difficile 630
Analyse The crystal structure of N-acetylmuramoyl-L-alanine amidase from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RN7
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylmuramoyl-L-alanine amidase
- EC
- 3.5.1.28
- UniProt
- Q183J9
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) | protein | 186 | 41% helix, 23% strand | Q183J9 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A
- FMT · Formic acid · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 4RN7 · The crystal structure of N-acetylmuramoyl-L-alanine amidase from Clostridium difficile 630 · 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 Q183J9
- Elsewhere: RCSB PDB 4RN7 · PDBe 4RN7 · UniProt Q183J9
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