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Cryo-EM structure of the drosophila CTP synthase product-bound filament

Analyse Cryo-EM structure of the drosophila CTP synthase product-bound filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6LFG
Type: protein
Length: 4,496 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CTP synthase
EC: 6.3.4.2
UniProt: Q9VUL1
Pockets: 20 · best druggability 0.89

Structure

electron microscopy · 1 distinct chain · 29% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, A, B, C, E, F, G, H	CTP synthase (EC 6.3.4.2)	protein	562	29% helix, 8% strand	Q9VUL1

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	990	0.89	0.91	140	empty
2	910	0.89	0.91	135	empty
3	957	0.89	0.90	130	empty
4	965	0.88	0.90	131	empty
5	914	0.88	0.90	114	empty

Interfaces

16 interfaces between chains.

F–G · 904 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 900 Å² buried · 5 hydrogen bonds · protein-protein
E–H · 875 Å² buried · 4 hydrogen bonds · protein-protein
D–C · 871 Å² buried · 4 hydrogen bonds · protein-protein
B–F · 639 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6LFG · Cryo-EM structure of the Drosophila CTP synthase product-bound filament · the same entry in another collection · chain H against H, TM-score 1.00
Q9VUL1 · AlphaFold monomer V2.0 prediction for CTP synthase (Q9VUL1) · a predicted model of the same protein · chain D against A, TM-score 0.90

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 Q9VUL1
Elsewhere: RCSB PDB 6LFG · PDBe 6LFG · UniProt Q9VUL1

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