4Q7J

Complex structure of viral RNA polymerase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003746	molecular_function	translation elongation factor activity
A	0005085	molecular_function	guanyl-nucleotide exchange factor activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
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
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	0016020	cellular_component	membrane
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	0000166	molecular_function	nucleotide binding
C	0001172	biological_process	RNA-templated transcription
C	0003723	molecular_function	RNA binding
C	0003968	molecular_function	RNA-directed RNA polymerase activity
C	0005515	molecular_function	protein binding
C	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0019079	biological_process	viral genome replication
C	0034062	molecular_function	5'-3' RNA polymerase activity
C	0039694	biological_process	viral RNA genome replication
C	0046872	molecular_function	metal ion binding
D	0003676	molecular_function	nucleic acid binding
E	0003746	molecular_function	translation elongation factor activity
E	0005085	molecular_function	guanyl-nucleotide exchange factor activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006412	biological_process	translation
E	0006414	biological_process	translational elongation
E	0008270	molecular_function	zinc ion binding
E	0016020	cellular_component	membrane
E	0032045	cellular_component	guanyl-nucleotide exchange factor complex
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0003723	molecular_function	RNA binding
F	0003746	molecular_function	translation elongation factor activity
F	0003924	molecular_function	GTPase activity
F	0005515	molecular_function	protein binding
F	0005525	molecular_function	GTP binding
F	0005737	cellular_component	cytoplasm
F	0005886	cellular_component	plasma membrane
F	0006412	biological_process	translation
F	0006414	biological_process	translational elongation
F	0016020	cellular_component	membrane
F	0016787	molecular_function	hydrolase activity
F	0032045	cellular_component	guanyl-nucleotide exchange factor complex
F	0046677	biological_process	response to antibiotic
F	0046872	molecular_function	metal ion binding
F	0097216	molecular_function	guanosine tetraphosphate 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
H	0003676	molecular_function	nucleic acid binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 601

Chain	Residue
B	SER219
B	SER221
C	GLU504
C	LEU505

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 602

Chain	Residue
B	HIS319
B	THR320
C	SER567
C	SER568
C	HOH761

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 601

Chain	Residue
F	SER219
F	SER221
G	GLU504
G	LEU505

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 602

Chain	Residue
F	HIS319
F	THR320
G	CYS566
G	SER567
G	SER568
G	HOH751

---

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
B	ASP50-SER65

---

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

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
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_FI7
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_FI8
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_FI9
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_FI10
Number of Residues	264
Details	Domain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20798060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22245970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22884418","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	132
Details	Domain: {"description":"S1 motif 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00180","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	132
Details	Domain: {"description":"S1 motif 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00180","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	4
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"37587340","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 535

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

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 535

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

---