Research workbench
Crystal structure of a semet derivative of amid at 2.2 ångströms
Analyse Crystal structure of a semet derivative of amid at 2.2 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BH7
- Type
- protein
- Length
- 254 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
- P75820
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) | protein | 254 | 33% helix, 18% strand | P75820 |
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 | 91 | 0.36 | 0.75 | 23 | ZN, SO4 |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2BH7 · Crystal structure of a SeMet derivative of AmiD at 2.2 angstroms · the same entry in another collection · chain A against A, TM-score 1.00
- P75820 · AlphaFold monomer V2.0 prediction for N-acetylmuramoyl-L-alanine amidase amid (P75820) · 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 P75820
- Elsewhere: RCSB PDB 2BH7 · PDBe 2BH7 · UniProt P75820
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