Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6N9U

Structure of bacteriophage T7 lagging-strand DNA polymerase (D5A/E7A) interacting with primase domains of two gp4 subunits bound to an RNA/DNA hybrid and dTTP (from LagS1)

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0003677	molecular_function	DNA binding
E	0003678	molecular_function	DNA helicase activity
E	0003697	molecular_function	single-stranded DNA binding
E	0003896	molecular_function	DNA primase activity
E	0004386	molecular_function	helicase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006260	biological_process	DNA replication
E	0006269	biological_process	DNA replication, synthesis of primer
E	0006996	biological_process	organelle organization
E	0008270	molecular_function	zinc ion binding
E	0016779	molecular_function	nucleotidyltransferase activity
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0032508	biological_process	DNA duplex unwinding
E	0039693	biological_process	viral DNA genome replication
E	0042802	molecular_function	identical protein binding
E	0043139	molecular_function	5'-3' DNA helicase activity
E	0046872	molecular_function	metal ion binding
E	1990077	cellular_component	primosome complex
F	0003677	molecular_function	DNA binding
F	0003678	molecular_function	DNA helicase activity
F	0003697	molecular_function	single-stranded DNA binding
F	0003896	molecular_function	DNA primase activity
F	0004386	molecular_function	helicase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006260	biological_process	DNA replication
F	0006269	biological_process	DNA replication, synthesis of primer
F	0006996	biological_process	organelle organization
F	0008270	molecular_function	zinc ion binding
F	0016779	molecular_function	nucleotidyltransferase activity
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0032508	biological_process	DNA duplex unwinding
F	0039693	biological_process	viral DNA genome replication
F	0042802	molecular_function	identical protein binding
F	0043139	molecular_function	5'-3' DNA helicase activity
F	0046872	molecular_function	metal ion binding
F	1990077	cellular_component	primosome complex
H	0000166	molecular_function	nucleotide binding
H	0003676	molecular_function	nucleic acid binding
H	0003677	molecular_function	DNA binding
H	0003887	molecular_function	DNA-directed DNA polymerase activity
H	0004527	molecular_function	exonuclease activity
H	0004529	molecular_function	DNA exonuclease activity
H	0005515	molecular_function	protein binding
H	0006260	biological_process	DNA replication
H	0006261	biological_process	DNA-templated DNA replication
H	0008408	molecular_function	3'-5' exonuclease activity
H	0039693	biological_process	viral DNA genome replication
H	0046872	molecular_function	metal ion binding
H	0090592	biological_process	DNA synthesis involved in DNA replication
H	0097681	biological_process	double-strand break repair via alternative nonhomologous end joining

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN E 601

Chain	Residue
E	CYS17
E	CYS20
E	CYS36
E	CYS39

site_id	AC2
Number of Residues	14
Details	binding site for residue TTP H 801

Chain	Residue
H	HIS506
H	ARG518
H	LYS522
H	TYR526
H	ASP654
H	MG802
P	DOC6
T	DA2004
T	DG2005
H	ASP475
H	ALA476
H	GLY478
H	LEU479
H	GLU480

site_id	AC3
Number of Residues	4
Details	binding site for residue MG H 802

Chain	Residue
H	ASP475
H	ALA476
H	ASP654
H	TTP801

site_id	AC4
Number of Residues	1
Details	binding site for residue MG H 803

Chain	Residue
H	HIS59

Functional Information from PROSITE/UniProt

site_id	PS00447
Number of Residues	20
Details	DNA_POLYMERASE_A DNA polymerase family A signature. RdnAKtfiYGflYgaGdekI

Chain	Residue	Details
H	ARG518-ILE537

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04101, ECO:0000305\|PubMed:9440688

Chain	Residue	Details
H	ASP5
H	GLU7
H	ASP174

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04101, ECO:0000269\|PubMed:9440688, ECO:0000305\|PubMed:9914251

Chain	Residue	Details
H	ASP475
F	ASP237
H	ALA476
H	ASP654
E	CYS39
E	ASP237
F	CYS17
F	CYS20
F	CYS36
F	CYS39

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04101, ECO:0000305\|PubMed:9914251

Chain	Residue	Details
H	HIS506
H	ARG518
H	LYS522
H	TYR526

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_04154

Chain	Residue	Details
E	SER312
F	SER312

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: dTTP/dATP binding => ECO:0000255\|HAMAP-Rule:MF_04154, ECO:0000305\|PubMed:10892646

Chain	Residue	Details
E	ARG361
F	ARG361

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: dTTP/dATP binding => ECO:0000255\|HAMAP-Rule:MF_04154, ECO:0000305\|PubMed:10535735

Chain	Residue	Details
E	HIS465
F	HIS465

site_id	SWS_FT_FI7
Number of Residues	6
Details	SITE: dTTP/dATP binding => ECO:0000255\|HAMAP-Rule:MF_04154, ECO:0000305\|PubMed:10535735, ECO:0000305\|PubMed:10892646

Chain	Residue	Details
E	ARG504
E	ARG522
E	TYR535
F	ARG504
F	ARG522
F	TYR535

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)