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Human dihydrofolate reductase complexed with NADPH and 5-{3-[3- methoxy-5-(isoquin-5-YL)PHENYL]PROP-1-yn-1-YL}6-ethylprimidine-2,4- diamine

Analyse Human dihydrofolate reductase complexed with NADPH and 5-{3-[3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KFJ
Type: protein
Length: 373 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P00374

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	186	—	P00374
B	—	protein	187	—	P00374

Compared structures

4KFJ · Human dihydrofolate reductase complexed with NADPH and… · the same entry in another collection · chain A against A, TM-score 1.00
P00374 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P00374) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P00374
Elsewhere: RCSB PDB 4KFJ · PDBe 4KFJ · UniProt P00374

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