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Crystal structure of TAM41 from firmicutes bacterium, complex with CTP-mg

Analyse Crystal structure of TAM41 from firmicutes bacterium, complex with CTP-mg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ECD
Type: protein
Length: 272 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphatidate cytidylyltransferase
EC: 2.7.7.41
UniProt: R5MX27
Ligands: CTP, MG, BR
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphatidate cytidylyltransferase (EC 2.7.7.41)	protein	272	50% helix, 16% strand	R5MX27

Ligands and binding sites

CTP · Cytidine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
BR · Bromide ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	416	0.69	0.81	35	CTP, MG
2	95	0.35	0.74	14	empty
3	75	0.30	0.73	17	empty

Compared structures

7ECD · Crystal structure of Tam41 from Firmicutes bacterium, complex with CTP-Mg · 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 R5MX27
Elsewhere: RCSB PDB 7ECD · PDBe 7ECD · UniProt R5MX27

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