MolNFT v1 · #37901 · protein

CP4 epsp synthase liganded with S3P

2GG6 · 3-phosphoshikimate 1-carboxyvinyltransferase: “CP4 epsp synthase liganded with S3P”. X-ray diffraction, 2 ligands (S3P, SO4), 2 pockets (best druggability 0.73). MolNFT v1 #37901 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 2GG6
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-phosphoshikimate 1-carboxyvinyltransferase
EC: 2.5.1.19
UniProt: Q9R4E4
Ligands: S3P, SO4
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19)	protein	445	33% helix, 28% strand	Q9R4E4

Ligands and binding sites

S3P · Shikimate-3-phosphate · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

2 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	170	0.73	0.91	39	SO4, S3P
2	89	0.47	0.81	17	empty

Compared structures

2GG6 · CP4 EPSP synthase liganded with S3P · the same entry in another collection · chain A against A, TM-score 1.00
Q9R4E4 · AlphaFold monomer V2.0 prediction for 3-phosphoshikimate 1-carboxyvinyltransferase… · a predicted model of the same protein · 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 Q9R4E4
Elsewhere: RCSB PDB 2GG6 · PDBe 2GG6 · UniProt Q9R4E4

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