MolNFT v1 · #81879 · protein

Structural and mechanistic studies of catalysis and sulfa drug resistance in dihydropteroate synthase

3V5O: “Structural and mechanistic studies of catalysis and sulfa drug resistance in dihydropteroate synthase”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.30). MolNFT v1 #81879 on GenesisL1: 3D structure, binding…

PDB: 3V5O
Type: protein
Length: 520 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: SO4
Pockets: 2 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydropteroate synthase (EC 2.5.1.15)	protein	262	48% helix, 15% strand	C3P9L8
B	Dihydropteroate synthase (EC 2.5.1.15)	protein	258	50% helix, 15% strand	C3P9L8

Ligands and binding sites

SO4 · Sulfate ion · ion · 11 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.30	0.75	12	empty
2	68	0.29	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 329 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3V5O · Structural and Mechanistic Studies of Catalysis and Sulfa Drug Resistance in… · 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 3V5O · PDBe 3V5O · UniProt C3P9L8

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