Research workbench
Enhancing DHFR catalysis by binding of an allosteric regulator nanobody (NB179)
Analyse Enhancing DHFR catalysis by binding of an allosteric regulator nanobody (NB179) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FHB
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase; NB179
- EC
- 1.5.1.3
- UniProt
- P0ABQ4
- Ligands
- FOL, NAP
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 159 | 23% helix, 31% strand | P0ABQ4 |
| D | NB179 | protein | 125 | 11% helix, 47% strand | — |
Ligands and binding sites
- FOL · Folic acid · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.66 | 0.79 | 31 | FOL |
| 2 | 60 | 0.37 | 0.79 | 13 | empty |
Interfaces
1 interface between chains.
- A–D · 660 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4FHB · Enhancing DHFR catalysis by binding of an allosteric regulator nanobody (Nb179) · the same entry in another collection · chain A against A, TM-score 1.00
- P0ABQ4 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P0ABQ4) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0ABQ4
- Elsewhere: RCSB PDB 4FHB · PDBe 4FHB · UniProt P0ABQ4
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