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Crystal structure of B. subtilis enga in complex with half-occupacy GDP

Analyse Crystal structure of B. subtilis enga in complex with half-occupacy GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DCT
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP-binding protein enga
UniProt: P50743
Ligands: GDP, SO4
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTP-binding protein enga	protein	401	37% helix, 23% strand	P50743

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A
SO4 · Sulfate ion · ion · 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	739	0.73	0.79	56	empty
2	177	0.70	0.88	36	empty
3	147	0.40	0.73	18	empty
4	70	0.29	0.74	20	empty

Compared structures

4DCT · Crystal Structure of B. subtilis EngA in complex with half-occupacy GDP · the same entry in another collection · chain A against A, TM-score 1.00
P50743 · AlphaFold monomer V2.0 prediction for GTPase der (P50743) · a predicted model of the same protein · chain A against A, TM-score 0.65

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 P50743
Elsewhere: RCSB PDB 4DCT · PDBe 4DCT · UniProt P50743

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