MolNFT v1 · #20285 · protein

Dihydrofolate reductase complexed with folate and 2- monophosphoadenosine 5'-diphosphoribose

1RA8: “Dihydrofolate reductase complexed with folate and 2- monophosphoadenosine 5'-diphosphoribose”. X-ray diffraction, 2 ligands (FOL, ATR), 1 pocket (best druggability 0.66). MolNFT v1 #20285 on GenesisL1: 3D structure, binding sites…

PDB: 1RA8
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: P0ABQ4
Ligands: FOL, ATR
Pockets: 1 · best druggability 0.66

Structure

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

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

Ligands and binding sites

FOL · Folic acid · ligand · chains A
ATR · 2'-monophosphoadenosine-5'-diphosphate · ligand · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	465	0.66	0.78	43	FOL, ATR

Compared structures

1RA8 · Dihydrofolate reductase complexed with folate and 2-monophosphoadenosine… · 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 1RA8 · PDBe 1RA8 · UniProt P0ABQ4

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