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Crystal structure of B. anthracis dhps with compound 19

Analyse Crystal structure of B. anthracis dhps with compound 19 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DAF
Type: protein
Length: 504 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydropteroate synthase
EC: 2.5.1.15
UniProt: C3P9L8
Ligands: 0J4, SO4
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydropteroate synthase (EC 2.5.1.15)	protein	252	51% helix, 15% strand	C3P9L8

Ligands and binding sites

0J4 · (2R)-2-(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 8 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.36	0.79	17	0J4

Interfaces

1 interface between chains.

A–B · 332 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

4DAF · Crystal structure of B. anthracis DHPS with compound 19 · 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 C3P9L8
Elsewhere: RCSB PDB 4DAF · PDBe 4DAF · UniProt C3P9L8

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