Research workbench
Dihydrofolate reductase from thermotoga maritima
Analyse Dihydrofolate reductase from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CZ3
- Type
- protein
- Length
- 332 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase
- EC
- 1.5.1.3
- UniProt
- Q60034
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 164 | 24% helix, 37% strand | Q60034 |
| B | Dihydrofolate reductase (EC 1.5.1.3) | protein | 168 | 23% helix, 36% strand | Q60034 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.64 | 0.79 | 33 | empty |
| 2 | 287 | 0.62 | 0.80 | 32 | empty |
| 3 | 124 | 0.45 | 0.77 | 24 | empty |
| 4 | 56 | 0.30 | 0.76 | 16 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1541 Ų buried · 23 hydrogen bonds · protein-protein
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 Q60034
- Elsewhere: RCSB PDB 1CZ3 · PDBe 1CZ3 · UniProt Q60034
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