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Crystal structure of T.TH. HB8 CTP synthetase complex with sulfate anion

Analyse Crystal structure of T.TH. HB8 CTP synthetase complex with sulfate anion in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1VCN
Type: protein
Length: 506 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CTP synthetase
EC: 6.3.4.2
UniProt: Q5SIA8
Ligands: SO4
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CTP synthetase (EC 6.3.4.2)	protein	506	40% helix, 22% strand	Q5SIA8

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

4 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	228	0.60	0.80	31	empty
2	277	0.54	0.76	46	SO4
3	90	0.45	0.80	16	empty
4	89	0.38	0.76	16	empty

Compared structures

1VCN · Crystal Structure of T.th. HB8 CTP synthetase complex with Sulfate anion · the same entry in another collection · chain A against A, TM-score 1.00
Q5SIA8 · AlphaFold monomer V2.0 prediction for CTP synthase (Q5SIA8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q5SIA8
Elsewhere: RCSB PDB 1VCN · PDBe 1VCN · UniProt Q5SIA8

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