SCOP 1.71: Domain d1euqa2: 1euq A:8-338

Lineage for d1euqa2 (1euq A:8-338)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.26: Adenine nucleotide alpha hydrolase-like [52373] (3 superfamilies)
   core: 3 layers, a/b/a ; parallel beta-sheet of 5 strands, order 32145

4. Superfamily c.26.1: Nucleotidylyl transferase [52374] (5 families)

5. Family c.26.1.1: Class I aminoacyl-tRNA synthetases (RS), catalytic domain [52375] (12 proteins)
   contains a conserved all-alpha subdomain at the C-terminal extension

6. Protein Glutaminyl-tRNA synthetase (GlnRS) [52380] (1 species)

7. Species Escherichia coli [TaxId:562] [52381] (13 PDB entries)

8. Domain d1euqa2: 1euq A:8-338 [31586]
   Other proteins in same PDB: d1euqa1
   protein/tRNA complex; complexed with qsi; mutant

Details for d1euqa2

PDB Entry: 1euq, 3.1 Å

PDB Description: crystal structure of glutaminyl-trna synthetase complexed with a trna-gln mutant and an active-site inhibitor

SCOP Domain Sequences for d1euqa2:

Sequence; same for both SEQRES and ATOM records:

>d1euqa2 c.26.1.1 (A:8-338) Glutaminyl-tRNA synthetase (GlnRS) {Escherichia coli}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen

Timeline for d1euqa2:

• d1euqa2 first appeared (with stable ids) in SCOP 1.55
  
• d1euqa2 appears in SCOP 1.69
  
• d1euqa2 appears in SCOP 1.73
  
• d1euqa2 appears in the current release, SCOPe 2.08