Research workbench
Crystal structure of a lysine racemase within internal aldimine linkage
Analyse Crystal structure of a lysine racemase within internal aldimine linkage in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DZA
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine racemase
- EC
- 5.1.1.5
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine racemase (EC 5.1.1.5) | protein | 371 | 38% helix, 25% strand | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.41 | 0.74 | 26 | empty |
| 2 | 62 | 0.30 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 4DZA · Crystal structure of a lysine racemase within internal aldimine linkage · 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
- Elsewhere: RCSB PDB 4DZA · PDBe 4DZA
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