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2.37 ångström structure of epsp synthase from acinetobacter baumannii

Analyse 2.37 ångström structure of epsp synthase from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5BUF
Type: protein
Length: 890 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-phosphoshikimate 1-carboxyvinyltransferase
EC: 2.5.1.19
UniProt: A0A0A7XPK6
Ligands: CL
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19)	protein	445	32% helix, 29% strand	A0A0A7XPK6

Ligands and binding sites

CL · Chloride ion · ion · 4 copies · chains A, B

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

Pockets

3 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	819	0.71	0.77	60	CL
2	651	0.69	0.77	67	CL
3	152	0.46	0.77	36	empty

Interfaces

1 interface between chains.

A–B · 627 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5BUF · 2.37 Angstrom Structure of EPSP Synthase from acinetobacter baumannii · 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 A0A0A7XPK6
Elsewhere: RCSB PDB 5BUF · PDBe 5BUF · UniProt A0A0A7XPK6

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