SCOPe 2.06: Domain d1x9na3: 1x9n A:534-753

Lineage for d1x9na3 (1x9n A:534-753)

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 folds)

3. Fold d.142: ATP-grasp [56058] (2 superfamilies)
   Consists of two subdomains with different alpha+beta folds
   shares functional and structural similarities with the PIPK and protein kinase superfamilies

4. Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (6 families)
   has a circularly permuted topology

5. Family d.142.2.1: ATP-dependent DNA ligase catalytic domain [56092] (2 proteins)
   automatically mapped to Pfam PF01068

6. Protein DNA ligase I (LIG1) [118122] (1 species)

7. Species Human (Homo sapiens) [TaxId:9606] [118123] (1 PDB entry)
   Uniprot P18858 262-901

8. Domain d1x9na3: 1x9n A:534-753 [115004]
   Other proteins in same PDB: d1x9na1, d1x9na2
   protein/DNA complex; complexed with amp

Details for d1x9na3

PDB Entry: 1x9n, 3 Å

PDB Description: Crystal Structure of Human DNA Ligase I bound to 5'-adenylated, nicked DNA

PDB Compounds: (A:) DNA ligase I

SCOPe Domain Sequences for d1x9na3:

Sequence; same for both SEQRES and ATOM records:

>d1x9na3 d.142.2.1 (A:534-753) DNA ligase I (LIG1) {Human (Homo sapiens) [TaxId: 9606]}
lspgiplkpmlahptrgisevlkrfeeaaftceykydgqraqihaleggevkifsrnqed
ntgkypdiisripkiklpsvtsfildteavawdrekkqiqpfqvlttrkrkevdaseiqv
qvclyafdliylngeslvreplsrrrqllrenfvetegefvfatsldtkdieqiaefleq
svkdsceglmvktldvdatyeiakrshnwlklkkdyldgv

Timeline for d1x9na3:

• d1x9na3 first appeared in SCOP 1.71
  
• d1x9na3 appears in SCOPe 2.05
  
• d1x9na3 appears in SCOPe 2.07
  
• d1x9na3 appears in the current release, SCOPe 2.08