Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SL0

Ternary 3' complex of T7 DNA polymerase with a DNA primer/template containing a disordered cis-syn thymine dimer on the template and an incoming nucleotide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003676	molecular_function	nucleic acid binding
A	0003677	molecular_function	DNA binding
A	0003824	molecular_function	catalytic activity
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0004518	molecular_function	nuclease activity
A	0004527	molecular_function	exonuclease activity
A	0004529	molecular_function	DNA exonuclease activity
A	0005515	molecular_function	protein binding
A	0006259	biological_process	DNA metabolic process
A	0006260	biological_process	DNA replication
A	0006261	biological_process	DNA-templated DNA replication
A	0006302	biological_process	double-strand break repair
A	0008408	molecular_function	3'-5' exonuclease activity
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0016787	molecular_function	hydrolase activity
A	0034061	molecular_function	DNA polymerase activity
A	0039693	biological_process	viral DNA genome replication
A	0046872	molecular_function	metal ion binding
A	0090592	biological_process	DNA synthesis involved in DNA replication
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0015035	molecular_function	protein-disulfide reductase activity
B	0030337	molecular_function	DNA polymerase processivity factor activity
B	0045454	biological_process	cell redox homeostasis
C	0000166	molecular_function	nucleotide binding
C	0003676	molecular_function	nucleic acid binding
C	0003677	molecular_function	DNA binding
C	0003824	molecular_function	catalytic activity
C	0003887	molecular_function	DNA-directed DNA polymerase activity
C	0004518	molecular_function	nuclease activity
C	0004527	molecular_function	exonuclease activity
C	0004529	molecular_function	DNA exonuclease activity
C	0005515	molecular_function	protein binding
C	0006259	biological_process	DNA metabolic process
C	0006260	biological_process	DNA replication
C	0006261	biological_process	DNA-templated DNA replication
C	0006302	biological_process	double-strand break repair
C	0008408	molecular_function	3'-5' exonuclease activity
C	0016740	molecular_function	transferase activity
C	0016779	molecular_function	nucleotidyltransferase activity
C	0016787	molecular_function	hydrolase activity
C	0034061	molecular_function	DNA polymerase activity
C	0039693	biological_process	viral DNA genome replication
C	0046872	molecular_function	metal ion binding
C	0090592	biological_process	DNA synthesis involved in DNA replication
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0015035	molecular_function	protein-disulfide reductase activity
D	0030337	molecular_function	DNA polymerase processivity factor activity
D	0045454	biological_process	cell redox homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 4003

Chain	Residue
A	ASP5
A	ASP65

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 4004

Chain	Residue
C	ASP5
C	HIS59
C	ASP65

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DAD C 4005

Chain	Residue
C	HIS506
C	ARG518

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DAD A 4004

Chain	Residue
A	TYR526
A	HIS506
A	ARG518

Functional Information from PROSITE/UniProt

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL

Chain	Residue	Details
B	LEU24-LEU42

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

Chain	Residue	Details
A	ARG518-ILE537

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9440688","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04101","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9914251","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Deprotonates C-terminal active site Cys"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Site: {"description":"Contributes to redox potential value"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
B	PRO34
B	CYS35
B	CYS32
B	GLY33

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
D	PRO34
D	CYS35
D	CYS32
D	GLY33

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
B	CYS35
B	CYS32

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1mek

Chain	Residue	Details
D	CYS35
D	CYS32

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