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Crystal structure analysis of sucrose hydrolase (suh)- tris complex

Analyse Crystal structure analysis of sucrose hydrolase (suh)- tris complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CZE
Type: protein
Length: 600 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sucrose hydrolase
EC: 3.2.1.48
UniProt: Q6UVM5
Pockets: 7 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sucrose hydrolase (EC 3.2.1.48)	protein	600	45% helix, 17% strand	Q6UVM5

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	444	0.63	0.77	43	TRS
2	194	0.51	0.77	28	empty
3	107	0.41	0.77	20	empty
4	96	0.38	0.76	16	empty
5	58	0.34	0.78	21	empty

Modifications

Observed in the structure: 13 modified (engineered).

Compared structures

3CZE · Crystal Structure Analysis of Sucrose hydrolase (SUH)- Tris complex · 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 Q6UVM5
Elsewhere: RCSB PDB 3CZE · PDBe 3CZE · UniProt Q6UVM5

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