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Structural dynamics and catalytic properties of a multi-modular xanthanase, native.

Analyse Structural dynamics and catalytic properties of a multi-modular xanthanase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FHJ
Type: protein
Length: 979 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PROTEIN,PROTEIN
Ligands: CA, NA, CL
Pockets: 8 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PROTEIN,PROTEIN	protein	979	23% helix, 29% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 5 copies · chains A
NA · Sodium ion · metal · 3 copies · chains A
CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
MLI · Malonate ion · additive · chains A

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

Pockets

8 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	764	0.70	0.77	76	MLI
2	410	0.62	0.77	57	empty
3	169	0.52	0.78	21	empty
4	135	0.43	0.76	27	empty
5	132	0.40	0.74	28	empty

Compared structures

6FHJ · Structural dynamics and catalytic properties of a multi-modular xanthanase, native. · 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
Elsewhere: RCSB PDB 6FHJ · PDBe 6FHJ

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