4R71

Structure of the Qbeta holoenzyme complex in the P1211 crystal form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003723	molecular_function	RNA binding
A	0003746	molecular_function	translation elongation factor activity
A	0003924	molecular_function	GTPase activity
A	0005085	molecular_function	guanyl-nucleotide exchange factor activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006412	biological_process	translation
A	0006414	biological_process	translational elongation
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0032045	cellular_component	guanyl-nucleotide exchange factor complex
A	0046677	biological_process	response to antibiotic
A	0097216	molecular_function	guanosine tetraphosphate binding
B	0000166	molecular_function	nucleotide binding
B	0001172	biological_process	RNA-templated transcription
B	0003723	molecular_function	RNA binding
B	0003968	molecular_function	RNA-dependent RNA polymerase activity
B	0005515	molecular_function	protein binding
B	0016740	molecular_function	transferase activity
B	0016779	molecular_function	nucleotidyltransferase activity
B	0019079	biological_process	viral genome replication
B	0034062	molecular_function	5'-3' RNA polymerase activity
B	0039694	biological_process	viral RNA genome replication
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003723	molecular_function	RNA binding
C	0003746	molecular_function	translation elongation factor activity
C	0003924	molecular_function	GTPase activity
C	0005085	molecular_function	guanyl-nucleotide exchange factor activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
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
C	0046677	biological_process	response to antibiotic
C	0097216	molecular_function	guanosine tetraphosphate binding
D	0000166	molecular_function	nucleotide binding
D	0001172	biological_process	RNA-templated transcription
D	0003723	molecular_function	RNA binding
D	0003968	molecular_function	RNA-dependent RNA polymerase activity
D	0005515	molecular_function	protein binding
D	0016740	molecular_function	transferase activity
D	0016779	molecular_function	nucleotidyltransferase activity
D	0019079	biological_process	viral genome replication
D	0034062	molecular_function	5'-3' RNA polymerase activity
D	0039694	biological_process	viral RNA genome replication
D	0046872	molecular_function	metal ion binding
E	0003676	molecular_function	nucleic acid binding
F	0003676	molecular_function	nucleic acid binding

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	ASP1051-SER1066

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

Chain	Residue	Details
A	LEU12-LEU27

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

Chain	Residue	Details
A	GLU75-LYS85

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418

Chain	Residue	Details
B	ASP274
B	ASP359
B	ASP360
D	ASP274
D	ASP359
D	ASP360

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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
A	SER1002
C	SER1001

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

Chain	Residue	Details
A	LYS1038
A	LYS1177
A	LYS1249
A	LYS1253
A	LYS1295
C	LYS1037
C	LYS1176
C	LYS1248
C	LYS1252
C	LYS1294

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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
A	LYS1057
C	LYS1056

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

Chain	Residue	Details
A	LYS1314
C	LYS1313

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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
A	THR1383
C	THR1382

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