SCOP 1.71: Domain d1pfva3: 1pfv A:141-175

Lineage for d1pfva3 (1pfv A:141-175)

1. Root: SCOP 1.71

2. Class g: Small proteins [56992] (79 folds)

3. Fold g.41: Rubredoxin-like [57769] (14 superfamilies)
   metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2

4. Superfamily g.41.1: Methionyl-tRNA synthetase (MetRS), Zn-domain [57770] (1 family)

5. Family g.41.1.1: Methionyl-tRNA synthetase (MetRS), Zn-domain [57771] (1 protein)
   in the Pyrococcus abyssi MetRS structure there is a tandem repeat of two such domains swapped with their zinc-binding 'knuckles', this duplicated finger occupies a larger region (124-183) than defined below; there is a structurally equivalent region in the E. coli enzyme lacking the second zinc-binding site

6. Protein Methionyl-tRNA synthetase (MetRS), Zn-domain [57772] (2 species)

7. Species Escherichia coli [TaxId:562] [57773] (9 PDB entries)

8. Domain d1pfva3: 1pfv A:141-175 [94662]
   Other proteins in same PDB: d1pfva1, d1pfva2
   complexed with 2fm, zn

Details for d1pfva3

PDB Entry: 1pfv, 1.7 Å

PDB Description: methionyl-trna synthetase from escherichia coli complexed with difluoromethionine

SCOP Domain Sequences for d1pfva3:

Sequence; same for both SEQRES and ATOM records:

>d1pfva3 g.41.1.1 (A:141-175) Methionyl-tRNA synthetase (MetRS), Zn-domain {Escherichia coli}
vkgtcpkckspdqygdncevcgatyspteliepks

Timeline for d1pfva3:

• d1pfva3 first appeared in SCOP 1.67
  
• d1pfva3 appears in SCOP 1.69
  
• d1pfva3 appears in SCOP 1.73
  
• d1pfva3 appears in the current release, SCOPe 2.08