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Room-temperature WT DHFR, time-averaged ensemble

Analyse Room-temperature WT DHFR, time-averaged ensemble in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4P3Q
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.351
Source: Escherichia coli
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: B1XC49
Ligands: FOL, NAP, CA
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.351 · 1 distinct chain · 26% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	26% helix, 34% strand	B1XC49

Ligands and binding sites

FOL · Folic acid · ligand · chains A
NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
CA · Calcium 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	440	0.73	0.83	47	FOL, NAP

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 B1XC49
Elsewhere: RCSB PDB 4P3Q · PDBe 4P3Q · UniProt B1XC49

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