MolNFT v1 · #103844 · protein

Multiconformer model for escherichia COLI dihydrofolate reductase at 277 K

4PST: “Multiconformer model for escherichia COLI dihydrofolate reductase at 277 K”. X-ray diffraction, 3 ligands (FOL, NAP, MN), 1 pocket (best druggability 0.70). MolNFT v1 #103844 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4PST
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
UniProt: U6N356
Ligands: FOL, NAP, MN
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase	protein	159	26% helix, 31% strand	U6N356

Ligands and binding sites

FOL · Folic acid · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · 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	321	0.70	0.83	43	FOL, NAP

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4PST · Multiconformer model for Escherichia coli dihydrofolate reductase at 277 K · the same entry in another collection · chain A against A, TM-score 1.00

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 U6N356
Elsewhere: RCSB PDB 4PST · PDBe 4PST · UniProt U6N356

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