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Contributions of orientation and hydrogen bonding to catalysis in asn- 229 mutants of thymidylate synthase

Analyse Contributions of orientation and hydrogen bonding to catalysis in asn- 229… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JMG
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: P00469
Ligands: UMP
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	316	40% helix, 22% strand	P00469

Ligands and binding sites

UMP · 2'-deoxyuridine 5'-monophosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	853	0.75	0.79	68	UMP

Compared structures

1JMG · Contributions of orientation and hydrogen bonding to catalysis in asn-229 mutants of… · the same entry in another collection · chain A against A, TM-score 1.00
P00469 · AlphaFold monomer V2.0 prediction for thymidylate synthase (P00469) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P00469
Elsewhere: RCSB PDB 1JMG · PDBe 1JMG · UniProt P00469

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