Research workbench
Alanine racemase
Analyse Alanine racemase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SFT
- Type
- protein
- Length
- 762 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanine racemase
- EC
- 5.1.1.1
- UniProt
- P10724
- Ligands
- PLP
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alanine racemase (EC 5.1.1.1) | protein | 382 | 32% helix, 27% strand | P10724 |
| B | Alanine racemase (EC 5.1.1.1) | protein | 380 | 33% helix, 27% strand | P10724 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.75 | 0.90 | 52 | PLP, ACT |
| 2 | 214 | 0.74 | 0.90 | 47 | ACT, PLP |
| 3 | 416 | 0.71 | 0.83 | 81 | empty |
| 4 | 57 | 0.68 | 0.95 | 23 | empty |
| 5 | 123 | 0.52 | 0.81 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 3349 Ų buried · 42 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
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 P10724
- Elsewhere: RCSB PDB 1SFT · PDBe 1SFT · UniProt P10724
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