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Methionine-free mutant of escherichia COLI dihydrofolate reductase

Analyse Methionine-free mutant of escherichia COLI dihydrofolate reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D0K
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: P00379
Ligands: FOL, CL
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	25% helix, 34% strand	P00379

Ligands and binding sites

FOL · Folic acid · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, 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	401	0.62	0.77	36	CL, FOL
2	298	0.59	0.77	29	FOL
3	215	0.46	0.74	21	empty
4	61	0.27	0.73	16	CL

Interfaces

1 interface between chains.

A–B · 65 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2D0K · Methionine-free mutant of Escherichia coli dihydrofolate reductase · 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 P00379
Elsewhere: RCSB PDB 2D0K · PDBe 2D0K · UniProt P00379

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