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Structure of obge from escherichia COLI

Analyse Structure of obge from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5M04
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTPase OBGE/CGTA
EC: 3.6.5.-
UniProt: P42641
Ligands: GDP, MG
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTPase OBGE/CGTA (EC 3.6.5.-)	protein	337	24% helix, 26% strand	P42641

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.72	0.93	17	empty
2	55	0.47	0.85	18	empty
3	106	0.47	0.79	16	empty
4	132	0.47	0.78	27	empty

Compared structures

5M04 · Structure of ObgE from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P42641 · AlphaFold monomer V2.0 prediction for GTPase OBGE/CGTA (P42641) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P42641
Elsewhere: RCSB PDB 5M04 · PDBe 5M04 · UniProt P42641

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