MolNFT v1 · #20419 · protein

Dihydrofolate reductase complexed with folate

1RE7: “Dihydrofolate reductase complexed with folate”. X-ray diffraction, 1 ligand (FOL), 3 pockets (best druggability 0.73). MolNFT v1 #20419 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1RE7
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P0ABQ4
Ligands: FOL
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	26% helix, 33% strand	P0ABQ4

Ligands and binding sites

FOL · Folic acid · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	679	0.73	0.79	52	FOL
2	605	0.71	0.79	40	FOL
3	68	0.30	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 542 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1RE7 · Dihydrofolate reductase complexed with folate · 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 0.98

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 P0ABQ4
Elsewhere: RCSB PDB 1RE7 · PDBe 1RE7 · UniProt P0ABQ4

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