1BPD

CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001701	biological_process	in utero embryonic development
A	0003677	molecular_function	DNA binding
A	0003684	molecular_function	damaged DNA binding
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005874	cellular_component	microtubule
A	0005876	cellular_component	spindle microtubule
A	0006260	biological_process	DNA replication
A	0006281	biological_process	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	0006915	biological_process	apoptotic process
A	0006954	biological_process	inflammatory response
A	0006974	biological_process	DNA damage response
A	0007435	biological_process	salivary gland morphogenesis
A	0008017	molecular_function	microtubule binding
A	0008630	biological_process	intrinsic apoptotic signaling pathway in response to DNA damage
A	0010332	biological_process	response to gamma radiation
A	0016445	biological_process	somatic diversification of immunoglobulins
A	0016446	biological_process	somatic hypermutation of immunoglobulin genes
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	0048535	biological_process	lymph node development
A	0048536	biological_process	spleen development
A	0048872	biological_process	homeostasis of number of cells
A	0051402	biological_process	neuron apoptotic process
A	0051575	molecular_function	5'-deoxyribose-5-phosphate lyase activity
A	0055093	biological_process	response to hyperoxia
A	0071707	biological_process	immunoglobulin heavy chain V-D-J recombination
A	0071897	biological_process	DNA biosynthetic process
A	0140078	molecular_function	class I DNA-(apurinic or apyrimidinic site) endonuclease activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 337

Chain	Residue
A	ARG149
A	SER180
A	GLY189

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	Region: {"description":"DNA-binding","evidences":[{"source":"UniProtKB","id":"P06746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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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":"UniProtKB","id":"P06746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P06746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K409","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Omega-N-methylarginine; by PRMT6","evidences":[{"source":"UniProtKB","id":"P06746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P06746","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP256

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