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Crystal structure of DHFR in 20% isopropanol

Analyse Crystal structure of DHFR in 20% isopropanol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5E8Q
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: C3TR70
Ligands: FOL, CA, CL
Pockets: 4 · best druggability 0.77

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	26% helix, 31% strand	C3TR70

Ligands and binding sites

FOL · Folic acid · ligand · 2 copies · chains B, A
CA · Calcium ion · metal · chains B
CL · Chloride ion · ion · 4 copies · chains B, A
IPA · Isopropyl alcohol · additive · chains B

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

Pockets

4 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	533	0.77	0.84	46	FOL, CL
2	524	0.74	0.82	48	FOL, CL
3	60	0.29	0.74	18	empty
4	69	0.29	0.73	16	IPA

Interfaces

1 interface between chains.

B–A · 581 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

5E8Q · Crystal structure of DHFR in 20% Isopropanol · the same entry in another collection · chain B against B, TM-score 1.00

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Every structure of UniProt C3TR70
Elsewhere: RCSB PDB 5E8Q · PDBe 5E8Q · UniProt C3TR70

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