Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3A5Z

Crystal structure of Escherichia coli GenX in complex with elongation factor P

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004824	molecular_function	lysine-tRNA ligase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006430	biological_process	lysyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0016880	molecular_function	acid-ammonia (or amide) ligase activity
A	0042803	molecular_function	protein homodimerization activity
A	0043687	biological_process	post-translational protein modification
A	0052868	molecular_function	protein-lysine lysyltransferase activity
A	0071468	biological_process	cellular response to acidic pH
B	0003746	molecular_function	translation elongation factor activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006414	biological_process	translational elongation
B	0043022	molecular_function	ribosome binding
B	0043043	biological_process	peptide biosynthetic process
B	0072344	biological_process	rescue of stalled ribosome
B	2001125	biological_process	negative regulation of translational frameshifting
C	0000049	molecular_function	tRNA binding
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004824	molecular_function	lysine-tRNA ligase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006430	biological_process	lysyl-tRNA aminoacylation
C	0016874	molecular_function	ligase activity
C	0016880	molecular_function	acid-ammonia (or amide) ligase activity
C	0042803	molecular_function	protein homodimerization activity
C	0043687	biological_process	post-translational protein modification
C	0052868	molecular_function	protein-lysine lysyltransferase activity
C	0071468	biological_process	cellular response to acidic pH
D	0003746	molecular_function	translation elongation factor activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006414	biological_process	translational elongation
D	0043022	molecular_function	ribosome binding
D	0043043	biological_process	peptide biosynthetic process
D	0072344	biological_process	rescue of stalled ribosome
D	2001125	biological_process	negative regulation of translational frameshifting
E	0000049	molecular_function	tRNA binding
E	0000166	molecular_function	nucleotide binding
E	0004812	molecular_function	aminoacyl-tRNA ligase activity
E	0004824	molecular_function	lysine-tRNA ligase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006418	biological_process	tRNA aminoacylation for protein translation
E	0006430	biological_process	lysyl-tRNA aminoacylation
E	0016874	molecular_function	ligase activity
E	0016880	molecular_function	acid-ammonia (or amide) ligase activity
E	0042803	molecular_function	protein homodimerization activity
E	0043687	biological_process	post-translational protein modification
E	0052868	molecular_function	protein-lysine lysyltransferase activity
E	0071468	biological_process	cellular response to acidic pH
F	0003746	molecular_function	translation elongation factor activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006412	biological_process	translation
F	0006414	biological_process	translational elongation
F	0043022	molecular_function	ribosome binding
F	0043043	biological_process	peptide biosynthetic process
F	0072344	biological_process	rescue of stalled ribosome
F	2001125	biological_process	negative regulation of translational frameshifting
G	0000049	molecular_function	tRNA binding
G	0000166	molecular_function	nucleotide binding
G	0004812	molecular_function	aminoacyl-tRNA ligase activity
G	0004824	molecular_function	lysine-tRNA ligase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006418	biological_process	tRNA aminoacylation for protein translation
G	0006430	biological_process	lysyl-tRNA aminoacylation
G	0016874	molecular_function	ligase activity
G	0016880	molecular_function	acid-ammonia (or amide) ligase activity
G	0042803	molecular_function	protein homodimerization activity
G	0043687	biological_process	post-translational protein modification
G	0052868	molecular_function	protein-lysine lysyltransferase activity
G	0071468	biological_process	cellular response to acidic pH
H	0003746	molecular_function	translation elongation factor activity
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006412	biological_process	translation
H	0006414	biological_process	translational elongation
H	0043022	molecular_function	ribosome binding
H	0043043	biological_process	peptide biosynthetic process
H	0072344	biological_process	rescue of stalled ribosome
H	2001125	biological_process	negative regulation of translational frameshifting

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE KAA A 990

Chain	Residue
A	GLU78
A	GLU244
A	LEU245
A	ASN247
A	PHE249
A	GLU251
A	ALA298
A	GLY300
A	HOH355
A	HOH360
B	GLY33
A	ARG100
A	GLU103
A	TYR107
A	HIS108
A	ASN109
A	PHE112
A	MET114
A	TYR118

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE KAA C 991

Chain	Residue
C	GLU78
C	ARG100
C	GLU103
C	TYR107
C	HIS108
C	ASN109
C	PHE112
C	MET114
C	TYR118
C	GLU244
C	LEU245
C	ASN247
C	PHE249
C	GLU251
C	GLY296
C	ALA298
C	GLY300
C	ARG303
D	GLY33

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE KAA E 992

Chain	Residue
E	GLU78
E	ARG100
E	GLU103
E	TYR107
E	HIS108
E	ASN109
E	PHE112
E	MET114
E	TYR118
E	GLU244
E	LEU245
E	ASN247
E	PHE249
E	GLU251
E	GLY296
E	GLY300
E	ARG303
F	GLY33

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE KAA G 993

Chain	Residue
G	GLU78
G	ARG100
G	GLU103
G	TYR107
G	HIS108
G	ASN109
G	PHE112
G	MET114
G	TYR118
G	GLU237
G	GLU244
G	LEU245
G	ASN247
G	PHE249
G	GLU251
G	GLY296
G	ALA298
G	GLY300
G	ARG303
G	HOH342

Functional Information from PROSITE/UniProt

site_id	PS01275
Number of Residues	20
Details	EFP Elongation factor P signature. KpAtlstGavVkVPlfVqiG

Chain	Residue	Details
B	LYS152-GLY171

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-(3,6-diaminohexanoyl)-5-hydroxylysine","evidences":[{"source":"PubMed","id":"21841797","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22128152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22706199","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)