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Crystal structure of an alginate lyase (BACOVA_01668) from bacteroides ovatus at 1.60 a resolution

Analyse Crystal structure of an alginate lyase (BACOVA_01668) from bacteroides ovatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NNB
Type: protein
Length: 380 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alginate lyase
UniProt: A7LV19
Ligands: NA
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alginate lyase	protein	380	57% helix, 4% strand	A7LV19

Ligands and binding sites

NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 2 copies · chains A
CIT · Citric acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	953	0.74	0.77	60	CIT, GOL
2	69	0.35	0.77	19	empty
3	60	0.34	0.77	18	GOL

Modifications

Observed in the structure: 17 modified (engineered).

Compared structures

3NNB · Crystal structure of an alginate lyase (BACOVA_01668) from Bacteroides ovatus at 1.60 A… · 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 A7LV19
Elsewhere: RCSB PDB 3NNB · PDBe 3NNB · UniProt A7LV19

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