8VZL

DNA Ligase 1 captured with pre-step 3 ligation at the rG:C nicksite

Functional Information from PROSITE/UniProt

site_id	PS00333
Number of Residues	27
Details	DNA_LIGASE_A2 ATP-dependent DNA ligase signature 2. EGLMVKtldvdat.YEiakrs.Hnwl..KLK

Chain	Residue	Details
A	GLU720-LYS746

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

Chain	Residue	Details
A	GLU566-ALA574

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: N6-AMP-lysine intermediate => ECO:0000255|PROSITE-ProRule:PRU10135

Chain	Residue	Details
A	LYS568

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15565146, ECO:0007744|PDB:1X9N

Chain	Residue	Details
A	GLU566
A	ARG573
A	LYS725
A	LYS744

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	GLU621
A	GLU720

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site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Interaction with target DNA

Chain	Residue	Details
A	ARG305
A	ASN590
A	LYS770
A	LYS795

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR798

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER801
A	SER819

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER911

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332

Chain	Residue	Details
A	SER913

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