MolNFT v1 · #2312 · protein

Thermostable thymidylate synthase a from bacillus subtilis

1BSP: “Thermostable thymidylate synthase a from bacillus subtilis”. X-ray diffraction, 1 ligand (PO4), 5 pockets (best druggability 0.77). MolNFT v1 #2312 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1BSP
Type: protein
Length: 555 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase a
EC: 2.1.1.45
UniProt: P42326
Ligands: PO4
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase a (EC 2.1.1.45)	protein	277	34% helix, 28% strand	P42326
B	Thymidylate synthase a (EC 2.1.1.45)	protein	278	32% helix, 27% strand	P42326

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	837	0.77	0.80	71	PO4
2	722	0.71	0.78	53	PO4
3	53	0.53	0.89	19	empty
4	57	0.48	0.85	19	empty
5	50	0.26	0.73	9	empty

Interfaces

1 interface between chains.

A–B · 2350 Å² buried · 53 hydrogen bonds · protein-protein

Compared structures

1BSP · Thermostable thymidylate synthase a from bacillus subtilis · 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 P42326
Elsewhere: RCSB PDB 1BSP · PDBe 1BSP · UniProt P42326

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