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Crystal structure of exotype alginate lyase ATU3025 H531A complexed with alginate trisaccharide

Analyse Crystal structure of exotype alginate lyase ATU3025 H531A complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AFL
Type: protein
Length: 766 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oligo alginate lyase
EC: 4.2.2.-
UniProt: A9CEJ9
Ligands: LGU, MAW
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oligo alginate lyase (EC 4.2.2.-)	protein	766	35% helix, 24% strand	A9CEJ9

Ligands and binding sites

LGU · alpha-L-gulopyranuronic acid · ligand · 2 copies · chains A
MAW · 4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid · ligand · chains A

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

Pockets

6 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	131	0.76	0.94	38	empty
2	420	0.71	0.82	53	LGU, MAW
3	347	0.67	0.81	35	empty
4	139	0.47	0.78	29	empty
5	133	0.47	0.78	25	empty

Compared structures

3AFL · Crystal structure of exotype alginate lyase Atu3025 H531A complexed with alginate… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A9CEJ9
Elsewhere: RCSB PDB 3AFL · PDBe 3AFL · UniProt A9CEJ9

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