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Crystal structure of sphingomonas sp. A1 alginate-binding protein ALGQ1 in complex with unsaturated trimannuronate

Analyse Crystal structure of sphingomonas sp. A1 alginate-binding protein ALGQ1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3A09
Type: protein
Length: 490 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALGQ1
UniProt: Q9KWT6
Ligands: MAV, MAW, BEM, CA
Pockets: 1 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALGQ1	protein	490	45% helix, 15% strand	Q9KWT6

Ligands and binding sites

MAV · alpha-D-mannopyranuronic acid · ligand · chains A
MAW · 4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid · ligand · chains A
BEM · beta-D-mannopyranuronic acid · sugar · chains A
CA · Calcium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1093	0.83	0.84	89	MAV, BEM, MAW

Compared structures

3A09 · Crystal structure of Sphingomonas sp. A1 alginate-binding protein AlgQ1 in complex with… · 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 Q9KWT6
Elsewhere: RCSB PDB 3A09 · PDBe 3A09 · UniProt Q9KWT6

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