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Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus.

Analyse Crystal Analysis Of Chorismate Mutase From Thermus Thermophilus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ODE
Type: protein
Length: 346 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.65
Source: THERMUS THERMOPHILUS
Molecule: Chorismate mutase
EC: 5.4.99.5
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · resolution 1.65 · 2 distinct chains · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chorismate mutase (EC 5.4.99.5)	protein	116	31% helix, 28% strand	—
B, C	Chorismate mutase (EC 5.4.99.5)	protein	115	30% helix, 30% strand	—

Pockets

3 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	217	0.63	0.83	27	empty
2	194	0.56	0.79	26	empty
3	187	0.53	0.79	28	empty

Interfaces

3 interfaces between chains.

A–B · 1073 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 1036 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 994 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1ODE · Crystal analysis of chorismate mutase from thermus thermophilus. · 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
Elsewhere: RCSB PDB 1ODE · PDBe 1ODE

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