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Crystal structure analysis of 3,6-anhydro-L-galactonate cycloisomerase

Analyse Crystal structure analysis of 3,6-anhydro-L-galactonate cycloisomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5XD9
Type: protein
Length: 362 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3,6-anhydro-alpha-L-galactonate cycloisomerase
EC: 5.5.1.25
UniProt: H2IFX0
Ligands: MG
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3,6-anhydro-alpha-L-galactonate cycloisomerase (EC 5.5.1.25)	protein	362	42% helix, 24% strand	H2IFX0

Ligands and binding sites

MG · Magnesium ion · metal · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.60	0.82	31	empty
2	71	0.57	0.88	23	empty
3	258	0.55	0.77	27	empty

Compared structures

5XD9 · Crystal structure analysis of 3,6-anhydro-L-galactonate cycloisomerase · the same entry in another collection · chain A against A, TM-score 1.00
H2IFX0 · AlphaFold monomer V2.0 prediction for 3,6-anhydro-alpha-L-galactonate cycloisomerase… · a predicted model of the same protein · 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 H2IFX0
Elsewhere: RCSB PDB 5XD9 · PDBe 5XD9 · UniProt H2IFX0

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