Research workbench

Electrostatics of active site microenvironments for E. COLI DHFR

Analyse Electrostatics of active site microenvironments for E. COLI DHFR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P68
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: C3TR70
Ligands: MTX, NAP, CA
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	24% helix, 34% strand	C3TR70

Ligands and binding sites

MTX · Methotrexate · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CA · Calcium ion · metal · 2 copies · chains A
ACT · Acetate ion · additive · 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	373	0.64	0.79	43	MTX, NAP

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

4P68 · Electrostatics of Active Site Microenvironments for E. coli DHFR · 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 C3TR70
Elsewhere: RCSB PDB 4P68 · PDBe 4P68 · UniProt C3TR70

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.