Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PC3

Elongation factor Tu:Ts complex with partially bound GDP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003723	molecular_function	RNA binding
A	0003746	molecular_function	translation elongation factor activity
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0016787	molecular_function	hydrolase activity
A	0032045	cellular_component	guanyl-nucleotide exchange factor complex
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003723	molecular_function	RNA binding
B	0003746	molecular_function	translation elongation factor activity
B	0003924	molecular_function	GTPase activity
B	0005515	molecular_function	protein binding
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0006412	biological_process	translation
B	0006414	biological_process	translational elongation
B	0016787	molecular_function	hydrolase activity
B	0032045	cellular_component	guanyl-nucleotide exchange factor complex
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
B	0097216	molecular_function	guanosine tetraphosphate binding
C	0003746	molecular_function	translation elongation factor activity
C	0005085	molecular_function	guanyl-nucleotide exchange factor activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006414	biological_process	translational elongation
C	0008270	molecular_function	zinc ion binding
C	0016020	cellular_component	membrane
C	0032045	cellular_component	guanyl-nucleotide exchange factor complex
D	0003746	molecular_function	translation elongation factor activity
D	0005085	molecular_function	guanyl-nucleotide exchange factor activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006414	biological_process	translational elongation
D	0008270	molecular_function	zinc ion binding
D	0016020	cellular_component	membrane
D	0032045	cellular_component	guanyl-nucleotide exchange factor complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue GDP A 401

Chain	Residue
A	HIS19
A	LYS136
A	ASP138
A	MET139
A	SER173
A	ALA174
A	LEU175
A	VAL20
A	ASP21
A	HIS22
A	GLY23
A	LYS24
A	THR25
A	THR26
A	ASN135

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL C 301

Chain	Residue
C	GLU193
C	GLN197
C	ARG218
C	LYS221
C	GLU225

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL C 302

Chain	Residue
C	GLN203
C	SER204
C	HOH416
C	HOH487
C	HOH524
D	GLU178
D	PHE179
D	HOH502

site_id	AC4
Number of Residues	13
Details	binding site for residue GDP B 401

Chain	Residue
B	HIS19
B	ASP21
B	GLY23
B	LYS24
B	THR25
B	THR26
B	ASN135
B	LYS136
B	ASP138
B	MET139
B	SER173
B	ALA174
B	LEU175

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL B 402

Chain	Residue
B	ARG58
B	ARG377
B	GLY380
B	ARG381
B	THR382
B	HOH578

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL D 301

Chain	Residue
C	GLU178
C	ILE180
D	GLN203
D	SER204
D	HOH422
D	HOH454
D	HOH496
D	HOH526

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL D 302

Chain	Residue
D	GLU193
D	GLN197
D	ARG218
D	LYS221
D	PHE222
D	GLU225

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. DNapeEKaRGITIntS

Chain	Residue	Details
A	ASP50-SER65

site_id	PS01126
Number of Residues	16
Details	EF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL

Chain	Residue	Details
C	LEU11-LEU26

site_id	PS01127
Number of Residues	11
Details	EF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK

Chain	Residue	Details
C	GLU74-LYS84

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Region: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"2022614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"389663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	6
Details	Region: {"description":"Involved in Mg(2+) ion dislocation from EF-Tu","evidences":[{"source":"HAMAP-Rule","id":"MF_00050","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 535

Chain	Residue	Details
A	ASP21	electrostatic stabiliser
A	LYS24	electrostatic stabiliser
A	THR25	metal ligand
A	HIS84	electrostatic stabiliser

site_id	MCSA2
Number of Residues	4
Details	M-CSA 535

Chain	Residue	Details
C	CYS22	electrostatic stabiliser
C	ALA25	electrostatic stabiliser
C	LEU26	metal ligand
C	ASP85	electrostatic stabiliser

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