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Staphylococcus aureus V31L, F98Y mutant dihydrofolate reductase complexed with NADPH

Analyse Staphylococcus aureus V31L, F98Y mutant dihydrofolate reductase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Q6A
Type: protein
Length: 157 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: W7NDF6
Ligands: NAP
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	157	20% helix, 35% strand	W7NDF6

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
GOL · Glycerol · additive · chains A
ACT · Acetate ion · additive · 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	324	0.67	0.81	44	NAP, GOL, ACT

Compared structures

4Q6A · Staphylococcus aureus V31L, F98Y Mutant Dihydrofolate Reductase Complexed with NADPH · 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 W7NDF6
Elsewhere: RCSB PDB 4Q6A · PDBe 4Q6A · UniProt W7NDF6

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