MolNFT v1 · #35046 · protein

Crystal structure of dihydropteroate synthase from thermus thermophilus HB8 in complex with 6HMPPP

2DZB: “Crystal structure of dihydropteroate synthase from thermus thermophilus HB8 in complex with 6HMPPP”. X-ray diffraction, 1 ligand (HH2), 2 pockets (best druggability 0.55). MolNFT v1 #35046 on GenesisL1: 3D structure, binding sites…

PDB: 2DZB
Type: protein
Length: 498 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydropteroate synthase
EC: 2.5.1.15
UniProt: Q5SLV2
Ligands: HH2
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydropteroate synthase (EC 2.5.1.15)	protein	251	47% helix, 17% strand	Q5SLV2
B	Dihydropteroate synthase (EC 2.5.1.15)	protein	247	43% helix, 17% strand	Q5SLV2

Ligands and binding sites

HH2 · 6-hydroxymethylpterin-diphosphate · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	241	0.55	0.78	35	HH2
2	209	0.54	0.78	37	HH2

Interfaces

1 interface between chains.

A–B · 1197 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2DZB · Crystal Structure of Dihydropteroate Synthase from Thermus thermophilus HB8 in complex… · 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 Q5SLV2
Elsewhere: RCSB PDB 2DZB · PDBe 2DZB · UniProt Q5SLV2

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