Research workbench
Crystal structure of putative dihydrodipicolinate synthase (TTHA0737) from thermus thermophilus HB8
Analyse Crystal structure of putative dihydrodipicolinate synthase (TTHA0737) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PCQ
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative dihydrodipicolinate synthase
- EC
- 4.2.1.52
- UniProt
- Q5SKB1
- Ligands
- K
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative dihydrodipicolinate synthase (EC 4.2.1.52) | protein | 283 | 52% helix, 12% strand | Q5SKB1 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.62 | 0.81 | 36 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2PCQ · Crystal structure of putative dihydrodipicolinate synthase (TTHA0737) from Thermus… · 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 Q5SKB1
- Elsewhere: RCSB PDB 2PCQ · PDBe 2PCQ · UniProt Q5SKB1
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