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Crystal structure of thymidylate synthase a from bacillus subtilis

Analyse Crystal structure of thymidylate synthase a from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B02
Type: protein
Length: 279 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (thymidylate synthase)
EC: 2.1.1.45
UniProt: P42326
Ligands: UFP, C2F
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (thymidylate synthase) (EC 2.1.1.45)	protein	279	34% helix, 27% strand	P42326

Ligands and binding sites

UFP · 5-fluoro-2'-deoxyuridine-5'-monophosphate · ligand · chains A
C2F · 5-methyl-5,6,7,8-tetrahydrofolic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	523	0.75	0.82	51	UFP, C2F
2	57	0.33	0.77	16	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

1B02 · Crystal structure of 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 1B02 · PDBe 1B02 · UniProt P42326

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