Research workbench
Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode
Analyse Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P4T
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dihydrofolate reductase type 2
- EC
- 1.5.1.3
- UniProt
- P00383
- Ligands
- NAP
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dihydrofolate reductase type 2 (EC 1.5.1.3) | protein | 58 | 5% helix, 45% strand | P00383 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2P4T · Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel… · the same entry in another collection · chain A against A, TM-score 1.00
- P00383 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase type 2 (P00383) · 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 P00383
- Elsewhere: RCSB PDB 2P4T · PDBe 2P4T · UniProt P00383
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