Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MMP

Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins

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
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
F	0000166	molecular_function	nucleotide binding
F	0001172	biological_process	RNA-templated transcription
F	0003723	molecular_function	RNA binding
F	0003968	molecular_function	RNA-directed RNA polymerase activity
F	0005515	molecular_function	protein binding
F	0016740	molecular_function	transferase activity
F	0016779	molecular_function	nucleotidyltransferase activity
F	0019079	biological_process	viral genome replication
F	0034062	molecular_function	5'-3' RNA polymerase activity
F	0039694	biological_process	viral RNA genome replication
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0001172	biological_process	RNA-templated transcription
G	0003723	molecular_function	RNA binding
G	0003968	molecular_function	RNA-directed RNA polymerase activity
G	0005515	molecular_function	protein binding
G	0016740	molecular_function	transferase activity
G	0016779	molecular_function	nucleotidyltransferase activity
G	0019079	biological_process	viral genome replication
G	0034062	molecular_function	5'-3' RNA polymerase activity
G	0039694	biological_process	viral RNA genome replication
G	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PXN A 1394

Chain	Residue
A	HOH741
A	HOH887
A	ARG1262
G	PRO143
G	MET148
G	TYR186
G	ALA189

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PXN C 1394

Chain	Residue
F	MET148
F	TYR186
C	ARG1262
F	PRO143

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	ASP1050-SER1065

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

Chain	Residue	Details
A	LEU11-LEU26

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

Chain	Residue	Details
A	GLU74-LYS84

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
G	ASP274
G	ASP359
G	ASP360
F	ASP274
F	ASP359
F	ASP360

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	SER1001
C	SER1001

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

Chain	Residue	Details
A	LYS1037
C	LYS1294
A	LYS1176
A	LYS1248
A	LYS1252
A	LYS1294
C	LYS1037
C	LYS1176
C	LYS1248
C	LYS1252

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	LYS1056
C	LYS1056

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

Chain	Residue	Details
A	LYS1313
C	LYS1313

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	THR1382
C	THR1382

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