1JMS

Crystal Structure of the Catalytic Core of Murine Terminal Deoxynucleotidyl Transferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003887	molecular_function	DNA-directed DNA polymerase activity
A	0006281	biological_process	DNA repair
A	0016779	molecular_function	nucleotidyltransferase activity
A	0034061	molecular_function	DNA polymerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 701

Chain	Residue
A	ASP343
A	ASP345
A	ASP434

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 702

Chain	Residue
A	THR253
A	VAL255
A	VAL258
A	HOH802

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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. GGFrRGkmtGhDVDFLItsP

Chain	Residue	Details
A	GLY332-PRO351

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Region: {"description":"Involved in DNA binding","evidences":[{"source":"PubMed","id":"11823435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23856622","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4I2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I2B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 11406636, 11823435, 7516580

Chain	Residue	Details
A	ASP434

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site_id	MCSA1
Number of Residues	3
Details	M-CSA 632

Chain	Residue	Details
A	ASP343	metal ligand
A	ASP345	metal ligand
A	ASP434	metal ligand, proton acceptor, proton donor

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