Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4J0Q

Crystal structure of Pseudomonas putida elongation factor Tu (EF-Tu)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion 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	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion 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	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006414	biological_process	translational elongation
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003746	molecular_function	translation elongation factor activity
C	0003924	molecular_function	GTPase activity
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006414	biological_process	translational elongation
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003746	molecular_function	translation elongation factor activity
D	0003924	molecular_function	GTPase activity
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006414	biological_process	translational elongation
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003746	molecular_function	translation elongation factor activity
E	0003924	molecular_function	GTPase activity
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006412	biological_process	translation
E	0006414	biological_process	translational elongation
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	THR26
A	GDP402
A	HOH513
A	HOH541
A	HOH542
A	HOH543

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GDP A 402

Chain	Residue
A	LYS25
A	THR26
A	THR27
A	ASN136
A	LYS137
A	ASP139
A	LEU140
A	SER174
A	ALA175
A	ARG176
A	MG401
A	HOH513
A	HOH516
A	HOH520
A	HOH528
A	HOH541
A	HOH542
A	HOH575
C	HOH585
A	ASP22
A	HIS23
A	GLY24

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MES A 403

Chain	Residue
A	ARG176
A	MET177
A	LYS182
A	ASP184
A	HOH549
C	ARG176
C	LYS182
C	ASP184
C	HOH548

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MPD A 404

Chain	Residue
A	GLY279
C	ASP110
C	MET113

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 405

Chain	Residue
A	ASP110
A	HOH579
B	MET264
B	PHE265
B	CYS278

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 401

Chain	Residue
B	THR26
B	GDP402
B	HOH511
B	HOH537
B	HOH538
B	HOH539

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE GDP B 402

Chain	Residue
B	ASP22
B	HIS23
B	GLY24
B	LYS25
B	THR26
B	THR27
B	ASN136
B	LYS137
B	ASP139
B	LEU140
B	SER174
B	ALA175
B	ARG176
B	MG401
B	HOH511
B	HOH517
B	HOH518
B	HOH529
B	HOH538
B	HOH539

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MES B 403

Chain	Residue
B	ARG176
B	MET177
B	LYS182
B	ASP184
B	HOH501
D	ARG176
D	LYS182
D	ASP184
D	HOH505

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 401

Chain	Residue
C	THR26
C	GDP402
C	HOH502
C	HOH508
C	HOH541
C	HOH549

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP C 402

Chain	Residue
C	MG401
C	HOH502
C	HOH516
C	HOH521
C	HOH541
C	HOH549
C	HOH566
C	HOH580
C	ASP22
C	HIS23
C	GLY24
C	LYS25
C	THR26
C	THR27
C	ASN136
C	LYS137
C	ASP139
C	LEU140
C	SER174
C	ALA175
C	ARG176

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD C 403

Chain	Residue
C	THR232
C	GLU263
C	PHE265
D	ASP110

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D 401

Chain	Residue
D	THR26
D	GDP402
D	HOH501
D	HOH502
D	HOH524
D	HOH525

site_id	BC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE GDP D 402

Chain	Residue
B	HOH516
D	ASP22
D	HIS23
D	GLY24
D	LYS25
D	THR26
D	THR27
D	ASN136
D	LYS137
D	ASP139
D	LEU140
D	SER174
D	ALA175
D	ARG176
D	MG401
D	HOH502
D	HOH510
D	HOH524
D	HOH529
D	HOH534
D	HOH556

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD D 403

Chain	Residue
D	THR232
D	GLU263
D	ASN277
D	CYS278
E	ASP110

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 401

Chain	Residue
E	THR26
E	GDP402
E	HOH501
E	HOH509
E	HOH510
E	HOH511

site_id	BC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE GDP E 402

Chain	Residue
E	HIS20
E	ASP22
E	HIS23
E	GLY24
E	LYS25
E	THR26
E	THR27
E	ASN136
E	LYS137
E	ASP139
E	LEU140
E	SER174
E	ALA175
E	ARG176
E	MG401
E	HOH501
E	HOH509
E	HOH511

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MES E 403

Chain	Residue
E	ASP139
E	ASP139
E	ARG176
E	ASP184
E	ASP184

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD E 404

Chain	Residue
B	ASP110
E	THR232

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. DSapeEKaRGITIntA

Chain	Residue	Details
A	ASP51-ALA66

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Region: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	15
Details	Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	15
Details	Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	10
Details	Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	75
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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