Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FMP

DNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003684	molecular_function	damaged DNA binding
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0003906	molecular_function	DNA-(apurinic or apyrimidinic site) endonuclease activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005874	cellular_component	microtubule
A	0005876	cellular_component	spindle microtubule
A	0006260	biological_process	DNA replication
A	0006261	biological_process	DNA-templated DNA replication
A	0006281	biological_process	DNA repair
A	0006282	biological_process	regulation of DNA repair
A	0006284	biological_process	base-excision repair
A	0006287	biological_process	base-excision repair, gap-filling
A	0006290	biological_process	pyrimidine dimer repair
A	0006297	biological_process	nucleotide-excision repair, DNA gap filling
A	0006303	biological_process	double-strand break repair via nonhomologous end joining
A	0006974	biological_process	DNA damage response
A	0008017	molecular_function	microtubule binding
A	0010332	biological_process	response to gamma radiation
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0016829	molecular_function	lyase activity
A	0019899	molecular_function	enzyme binding
A	0032991	cellular_component	protein-containing complex
A	0034061	molecular_function	DNA polymerase activity
A	0045471	biological_process	response to ethanol
A	0046872	molecular_function	metal ion binding
A	0051575	molecular_function	5'-deoxyribose-5-phosphate lyase activity
A	0055093	biological_process	response to hyperoxia
A	0070421	cellular_component	DNA ligase III-XRCC1 complex
A	0071897	biological_process	DNA biosynthetic process
A	0090734	cellular_component	site of DNA damage
A	0140078	molecular_function	class I DNA-(apurinic or apyrimidinic site) endonuclease activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1339

Chain	Residue
A	ASP190
A	ASP192
A	DCT1338
A	NA1340
A	HOH1408
A	HOH1409

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1340

Chain	Residue
A	DCT1338
A	MG1339
P	HOH11
A	ASP190
A	ASP192
A	ASP256

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1341

Chain	Residue
A	THR101
A	VAL103
A	ILE106
A	HOH1410
P	DG9
P	HOH12

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1342

Chain	Residue
A	LYS60
A	LEU62
A	VAL65
A	HOH1411
D	DC3
D	HOH6

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 1402

Chain	Residue
A	ARG126
A	NA1406
A	HOH1493
A	HOH1501
A	HOH1510
A	HOH1526
A	HOH1569

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 1406

Chain	Residue
A	NA1402
A	HOH1499
A	HOH1501
A	HOH1510
A	HOH1526
A	HOH1528
A	HOH1558

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE DCT A 1338

Chain	Residue
A	GLY179
A	SER180
A	ARG183
A	GLY189
A	ASP190
A	ASP192
A	TYR271
A	PHE272
A	GLY274
A	ASP276
A	ASN279
A	MG1339
A	NA1340
A	HOH1407
A	HOH1408
A	HOH1409
A	HOH1419
A	HOH1427
A	HOH1440
A	HOH1568
A	HOH1602
A	HOH1667
A	HOH1707
A	HOH1777
P	DOC10
P	HOH11
T	DG6

Functional Information from PROSITE/UniProt

site_id	PS00522
Number of Residues	20
Details	DNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP

Chain	Residue	Details
A	GLY179-PRO198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Region: {"description":"DNA-binding"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity","evidences":[{"source":"PubMed","id":"9572863","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12517346","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8841120","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9287163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BPX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BPZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MQ3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZQO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZQQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8841119","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ICW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8ICX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8ICY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8841119","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ICX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9287163","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BPY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K409","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine; by PRMT6","evidences":[{"source":"PubMed","id":"16600869","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19713937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21362556","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP256

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