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Crystal structure of PH1733, an aspartate racemase homologue, from pyrococcus horikoshii OT3
Analyse Crystal structure of PH1733, an aspartate racemase homologue, from pyrococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZSK
- Type
- protein
- Length
- 452 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 226AA long hypothetical aspartate racemase
- UniProt
- O59384
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 226AA long hypothetical aspartate racemase | protein | 226 | 54% helix, 14% strand | O59384 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 354 | 0.66 | 0.80 | 35 | empty |
| 2 | 311 | 0.60 | 0.78 | 41 | empty |
| 3 | 172 | 0.45 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1511 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2ZSK · Crystal structure of PH1733, an aspartate racemase homologue, from Pyrococcus horikoshii… · 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 O59384
- Elsewhere: RCSB PDB 2ZSK · PDBe 2ZSK · UniProt O59384
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