Research workbench
Crystal structure of N-acylamino acid racemase from thermus thermophilus HB8
Analyse Crystal structure of N-acylamino acid racemase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZC8
- Type
- protein
- Length
- 736 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acylamino acid racemase
- UniProt
- Q5SJX8
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | N-acylamino acid racemase | protein | 368 | 38% helix, 24% strand | Q5SJX8 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 784 | 0.79 | 0.82 | 77 | empty |
| 2 | 609 | 0.77 | 0.83 | 60 | empty |
| 3 | 677 | 0.77 | 0.82 | 60 | empty |
| 4 | 65 | 0.69 | 0.95 | 14 | empty |
| 5 | 129 | 0.40 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1575 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2ZC8 · Crystal structure of N-Acylamino Acid Racemase from Thermus thermophilus HB8 · 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 Q5SJX8
- Elsewhere: RCSB PDB 2ZC8 · PDBe 2ZC8 · UniProt Q5SJX8
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