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Crystal structure analysis of CYS167 mutant of escherichia COLI

Analyse Crystal structure analysis of CYS167 mutant of escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EV8
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate synthase
EC: 2.1.1.45
UniProt: P0A884
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate synthase (EC 2.1.1.45)	protein	264	34% helix, 26% strand	P0A884

Pockets

3 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	546	0.69	0.78	52	empty
2	59	0.34	0.77	18	empty
3	64	0.29	0.73	15	empty

Modifications

Observed in the structure: 5 modified (artifact, carboxylation).

Compared structures

1EV8 · Crystal structure analysis of CYS167 mutant of escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P0A884 · AlphaFold monomer V2.0 prediction for thymidylate synthase (P0A884) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P0A884
Elsewhere: RCSB PDB 1EV8 · PDBe 1EV8 · UniProt P0A884

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