2HVQ

Structure of Adenylated full-length T4 RNA Ligase 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003972	molecular_function	RNA ligase (ATP) activity
A	0005524	molecular_function	ATP binding
A	0016874	molecular_function	ligase activity
A	0042245	biological_process	RNA repair
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 335

Chain	Residue
A	APK35
A	HIS37
A	GLU204
A	HOH391
A	HOH410

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 336

Chain	Residue
A	HOH352
A	ILE162
A	LEU164
A	ASN166
A	TYR206

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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|HAMAP-Rule:MF_04150, ECO:0000269|PubMed:17018278

Chain	Residue	Details
A	APK35

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04150, ECO:0000269|PubMed:14962393, ECO:0000269|PubMed:17018278

Chain	Residue	Details
A	GLU34
A	ILE36
A	ASN40
A	GLU99
A	LYS225
A	LYS227

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:14962393, ECO:0000269|PubMed:17018278

Chain	Residue	Details
A	APK35

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04150, ECO:0000269|PubMed:14962393

Chain	Residue	Details
A	ARG55

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site_id	SWS_FT_FI5
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04150, ECO:0000269|PubMed:17018278

Chain	Residue	Details
A	ILE162
A	LEU164
A	ASN166
A	GLU204
A	TYR206

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Interaction with RNA => ECO:0000255|HAMAP-Rule:MF_04150

Chain	Residue	Details
A	ASN218
A	LYS314

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