Research workbench

Staphylococcus aureus S1:DHFR

Analyse Staphylococcus aureus S1:DHFR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W9T
Type: protein
Length: 318 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase type 1
EC: 1.5.1.3
UniProt: P13955
Pockets: 4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrofolate reductase type 1 (EC 1.5.1.3)	protein	159	18% helix, 32% strand	P13955

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	62	0.62	0.92	23	empty
2	59	0.59	0.91	20	empty
3	94	0.41	0.77	14	empty
4	52	0.26	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1149 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

2W9T · Staphylococcus aureus S1:DHFR · the same entry in another collection · chain A against A, TM-score 1.00
P13955 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase type 1 from TN4003 (P13955) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P13955
Elsewhere: RCSB PDB 2W9T · PDBe 2W9T · UniProt P13955

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