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Crystal structure of yeast ESA1(C304S) mutant complexed with coenzyme a

Analyse Crystal structure of yeast ESA1(C304S) mutant complexed with coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MJ9
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ESA1 protein
UniProt: Q08649
Ligands: COA, NA
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ESA1 protein	protein	273	36% helix, 25% strand	Q08649

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
NA · Sodium ion · metal · chains A

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

Pockets

4 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	628	0.72	0.79	68	NA, COA
2	68	0.42	0.80	19	empty
3	74	0.37	0.78	18	empty
4	69	0.37	0.78	18	empty

Compared structures

1MJ9 · Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A · the same entry in another collection · chain A against A, TM-score 1.00
Q08649 · AlphaFold monomer V2.0 prediction for histone acetyltransferase ESA1 (Q08649) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q08649
Elsewhere: RCSB PDB 1MJ9 · PDBe 1MJ9 · UniProt Q08649

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