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Crystal structure of the trehalulose synthase mutb from pseudomonas mesoacidophila mx-45

Analyse Crystal structure of the trehalulose synthase mutb from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PWH
Type: protein
Length: 1,112 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sucrose isomerase
EC: 5.4.99.1
UniProt: Q2PS28
Ligands: CA
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Sucrose isomerase (EC 5.4.99.1)	protein	556	33% helix, 19% strand	Q2PS28

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.77	0.98	21	empty
2	92	0.76	0.97	21	empty
3	246	0.58	0.79	26	empty
4	206	0.56	0.79	25	empty
5	155	0.46	0.76	24	empty

Interfaces

1 interface between chains.

A–B · 229 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2PWH · Crystal structure of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45 · 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 Q2PS28
Elsewhere: RCSB PDB 2PWH · PDBe 2PWH · UniProt Q2PS28

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