1DG1

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

Functional Information from GO Data

Chain	GOid	namespace	contents
G	0003723	molecular_function	RNA binding
G	0003746	molecular_function	translation elongation factor activity
G	0003924	molecular_function	GTPase activity
G	0005515	molecular_function	protein binding
G	0005525	molecular_function	GTP binding
G	0005737	cellular_component	cytoplasm
G	0005886	cellular_component	plasma membrane
G	0006412	biological_process	translation
G	0006414	biological_process	translational elongation
G	0032045	cellular_component	guanyl-nucleotide exchange factor complex
G	0046677	biological_process	response to antibiotic
G	0097216	molecular_function	guanosine tetraphosphate binding
H	0003723	molecular_function	RNA binding
H	0003746	molecular_function	translation elongation factor activity
H	0003924	molecular_function	GTPase activity
H	0005515	molecular_function	protein binding
H	0005525	molecular_function	GTP binding
H	0005737	cellular_component	cytoplasm
H	0005886	cellular_component	plasma membrane
H	0006412	biological_process	translation
H	0006414	biological_process	translational elongation
H	0032045	cellular_component	guanyl-nucleotide exchange factor complex
H	0046677	biological_process	response to antibiotic
H	0097216	molecular_function	guanosine tetraphosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG G 998

Chain	Residue
G	THR25
G	GDP999
G	HOH1002
G	HOH1003
G	HOH1004
G	HOH1006

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG H 998

Chain	Residue
H	HOH2028
H	HOH2029
H	HOH2030
H	HOH2033
H	THR25
H	ASP80
H	GDP1999

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GDP G 999

Chain	Residue
G	VAL20
G	ASP21
G	HIS22
G	GLY23
G	LYS24
G	THR25
G	THR26
G	ASN135
G	LYS136
G	ASP138
G	MET139
G	SER173
G	ALA174
G	LEU175
G	MG998
G	HOH1002
G	HOH1003

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE GDP H 1999

Chain	Residue
H	VAL20
H	ASP21
H	HIS22
H	GLY23
H	LYS24
H	THR25
H	THR26
H	ASN135
H	LYS136
H	ASP138
H	SER173
H	ALA174
H	LEU175
H	MG998
H	HOH2029
H	HOH2030
H	HOH2033
H	HOH2034
H	HOH2035

---

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
G	ASP50-SER65

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
G	GLY18
G	ASP80
G	ASN135
H	GLY18
H	ASP80
H	ASN135

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545

Chain	Residue	Details
G	SER1
H	SER1

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
G	LYS37
H	LYS294
G	LYS176
G	LYS248
G	LYS252
G	LYS294
H	LYS37
H	LYS176
H	LYS248
H	LYS252

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545

Chain	Residue	Details
G	LYS56
H	LYS56

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
G	LYS313
H	LYS313

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965

Chain	Residue	Details
G	THR382
H	THR382

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
G	ASP21

---

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
H	ASP21

---

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
G	HIS84

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site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1ksj

Chain	Residue	Details
H	HIS84

---