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Crystal structure of putative fructose-1,6-bisphosphate aldolase from candida auris

Analyse Crystal structure of putative fructose-1,6-bisphosphate aldolase from candida… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RGN
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase
EC: 4.1.2.13
UniProt: A0A5C1DZF7
Ligands: ZN
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	340	50% helix, 12% strand	A0A5C1DZF7

Ligands and binding sites

ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · chains A
IPA · Isopropyl alcohol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	112	0.40	0.76	19	empty
2	71	0.34	0.76	14	empty

Compared structures

7RGN · Crystal structure of putative fructose-1,6-bisphosphate aldolase from Candida auris · 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 A0A5C1DZF7
Elsewhere: RCSB PDB 7RGN · PDBe 7RGN · UniProt A0A5C1DZF7

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