6N0I

2.60 Angstrom Resolution Crystal Structure of Elongation Factor G 2 from Pseudomonas putida.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003746	molecular_function	translation elongation factor activity
A	0003924	molecular_function	GTPase activity
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0032790	biological_process	ribosome disassembly
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000166	molecular_function	nucleotide binding
B	0003746	molecular_function	translation elongation factor activity
B	0003924	molecular_function	GTPase activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0006412	biological_process	translation
B	0006414	biological_process	translational elongation
B	0032790	biological_process	ribosome disassembly
B	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue SO4 A 801

Chain	Residue
A	GLU229
A	GLU261

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site_id	AC2
Number of Residues	3
Details	binding site for residue SO4 B 801

Chain	Residue
B	GLU229
B	ALA230
B	GLU261

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site_id	AC3
Number of Residues	2
Details	binding site for residue PEG B 802

Chain	Residue
B	GLU316
B	LYS403

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Functional Information from PROSITE/UniProt

site_id	PS00301
Number of Residues	16
Details	G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DWmaqEQeRGITItsA

Chain	Residue	Details
A	ASP51-ALA66

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00054","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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