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Alternate binding modes observed for the E- and Z-isomers of 2,4- DIAMINOFURO[2,3-D]PYRIMIDINES as ternary complexes with NADPH and mouse dihydrofolate reductase

Analyse Alternate binding modes observed for the E- and Z-isomers of 2,4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3K47
Type: protein
Length: 186 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00375

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	186	—	P00375

Compared structures

3K47 · Alternate Binding Modes Observed for the E- and Z-Isomers of… · the same entry in another collection · chain A against A, TM-score 1.00
P00375 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00375) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P00375
Elsewhere: RCSB PDB 3K47 · PDBe 3K47 · UniProt P00375

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