Research workbench
R104A-CA1697 nanobody binding to the binary DHFR.FOLATE complex
Analyse R104A-CA1697 nanobody binding to the binary DHFR.FOLATE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I1N
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase; Protein CA1697 (nanobody)
- EC
- 1.5.1.3
- UniProt
- P0ABQ4
- Ligands
- FOL
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase (EC 1.5.1.3) | protein | 159 | 26% helix, 30% strand | P0ABQ4 |
| B | Protein CA1697 (nanobody) | protein | 128 | 9% helix, 47% strand | — |
Ligands and binding sites
- FOL · Folic acid · 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 | 484 | 0.76 | 0.84 | 51 | FOL |
| 2 | 135 | 0.42 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 648 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P0ABQ4
- Elsewhere: RCSB PDB 4I1N · PDBe 4I1N · UniProt P0ABQ4
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