6IML

The crystal structure of AsfvLIG:CT1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003909	molecular_function	DNA ligase activity
A	0003910	molecular_function	DNA ligase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0006260	biological_process	DNA replication
A	0006281	biological_process	DNA repair
A	0006310	biological_process	DNA recombination
A	0006974	biological_process	DNA damage response
A	0016874	molecular_function	ligase activity
A	0044423	cellular_component	virion component
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division

Functional Information from PROSITE/UniProt

site_id	PS00333
Number of Residues	28
Details	DNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGAIVRnangp...YEpgynnyHsahlaKLK

Chain	Residue	Details
A	GLU291-LYS318

---

site_id	PS00697
Number of Residues	9
Details	DNA_LIGASE_A1 ATP-dependent DNA ligase AMP-binding site. QRKRNGVRA

Chain	Residue	Details
A	GLN149-ALA157

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"N6-AMP-lysine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10135","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Site: {"description":"Important for the catalytic efficiency","evidences":[{"source":"PubMed","id":"30674878","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---