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The crystal structure of 4-diphosphocytidyl-2C-methyl-D- erythritolsynthase from anaerococcus prevotii dsm 20548

Analyse The crystal structure of 4-diphosphocytidyl-2C-methyl-D- erythritolsynthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KT7
Type: protein
Length: 446 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
EC: 2.7.7.60
UniProt: C7RFG6
Ligands: NA, CL
Pockets: 1 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60)	protein	227	34% helix, 27% strand	C7RFG6
B	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60)	protein	219	37% helix, 27% strand	C7RFG6

Ligands and binding sites

NA · Sodium ion · metal · chains A, B
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1200	0.77	0.79	95	empty

Interfaces

1 interface between chains.

A–B · 2017 Å² buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4KT7 · The crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritolsynthase from… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt C7RFG6
Elsewhere: RCSB PDB 4KT7 · PDBe 4KT7 · UniProt C7RFG6

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