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Crystal structure of the R395G mutant form of coronafacic acid ligase from pectobacterium brasiliense

Analyse Crystal structure of the R395G mutant form of coronafacic acid ligase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A9J
Type: protein
Length: 503 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cfl
UniProt: M4GWN4
Ligands: R4Z, PO4
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cfl	protein	503	35% helix, 27% strand	M4GWN4

Ligands and binding sites

R4Z · 6-ethyl-1-oxidanylidene-indene-4-carboxylic acid · ligand · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	388	0.62	0.77	45	empty
2	405	0.61	0.76	58	R4Z, PO4
3	116	0.41	0.76	22	empty

Compared structures

7A9J · Crystal structure of the R395G mutant form of Coronafacic Acid Ligase from Pectobacterium… · 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 M4GWN4
Elsewhere: RCSB PDB 7A9J · PDBe 7A9J · UniProt M4GWN4

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