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Structure of the 2-methylcitrate synthase (prpc) from coxiella burnetii

Analyse Structure of the 2-methylcitrate synthase (prpc) from coxiella burnetii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TQG
Type: protein
Length: 722 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-methylcitrate synthase
EC: 2.3.3.5
UniProt: Q83DG4
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 61% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-methylcitrate synthase (EC 2.3.3.5)	protein	360	61% helix, 5% strand	Q83DG4
B	2-methylcitrate synthase (EC 2.3.3.5)	protein	362	60% helix, 4% strand	Q83DG4

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	463	0.70	0.80	47	empty
2	508	0.69	0.79	48	empty
3	70	0.39	0.78	14	empty
4	84	0.35	0.75	23	empty
5	62	0.34	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 3774 Å² buried · 65 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

3TQG · Structure of the 2-methylcitrate synthase (prpC) from Coxiella burnetii · 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 Q83DG4
Elsewhere: RCSB PDB 3TQG · PDBe 3TQG · UniProt Q83DG4

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