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Crystal structure of streptococcus pneumoniae dihydrofolate reductase - SP9 mutant

Analyse Crystal structure of streptococcus pneumoniae dihydrofolate reductase - SP9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IX9
Type: protein
Length: 332 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: O85261
Ligands: NDP, MTX
Pockets: 2 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrofolate reductase (EC 1.5.1.3)	protein	166	23% helix, 35% strand	O85261

Ligands and binding sites

NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
MTX · Methotrexate · ligand · 2 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1151	0.84	0.85	107	NDP, MTX
2	71	0.38	0.78	14	empty

Interfaces

1 interface between chains.

A–B · 899 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3IX9 · Crystal structure of Streptococcus pneumoniae dihydrofolate reductase - Sp9 mutant · 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 O85261
Elsewhere: RCSB PDB 3IX9 · PDBe 3IX9 · UniProt O85261

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