Research workbench

Moritella profunda dihydrofolate reductase (DHFR)

Analyse Moritella profunda dihydrofolate reductase (DHFR) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IA5
Type: protein
Length: 320 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: Q70YQ6
Ligands: PO4
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	159	26% helix, 35% strand	Q70YQ6
B	Dihydrofolate reductase (EC 1.5.1.3)	protein	161	25% helix, 35% strand	Q70YQ6

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains A, B

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

Pockets

2 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	708	0.73	0.79	70	PO4
2	410	0.67	0.79	40	PO4

Interfaces

1 interface between chains.

A–B · 428 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3IA5 · Moritella profunda dihydrofolate reductase (DHFR) · the same entry in another collection · chain B against B, 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 Q70YQ6
Elsewhere: RCSB PDB 3IA5 · PDBe 3IA5 · UniProt Q70YQ6

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