MolNFT v1 · #146382 · protein
Crystal structures of escherichia COLI dihydrofolate reductase. the NADP+ holoenzyme and the FOLATE(DOT)NADP+ ternary complex. substrate binding and a model for the transition state
6DFR: “Crystal structures of escherichia COLI dihydrofolate reductase. the NADP+ holoenzyme and the FOLATE(DOT)NADP+…”. X-ray diffraction, 2 ligands (NAP, CA). MolNFT v1 #146382 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DFR
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0ABQ4
- Ligands
- NAP, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 154 | — | P0ABQ4 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DFR · Crystal structures of escherichia COLI dihydrofolate reductase. the NADP+ holoenzyme and… · 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 6DFR · PDBe 6DFR · UniProt P0ABQ4
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