SCOP 1.75: Domain d2p50c1: 2p50 C:1-53,C:351-382

Lineage for d2p50c1 (2p50 C:1-53,C:351-382)

1. Root: SCOP 1.75

2. Class b: All beta proteins [48724] (174 folds)

3. Fold b.92: Composite domain of metallo-dependent hydrolases [51337] (1 superfamily)
   pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns

4. Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (11 families)
   this domain is interrupted by the catalytic beta/alpha barrel domain

5. Family b.92.1.5: N-acetylglucosamine-6-phosphate deacetylase, NagA [82227] (1 protein)

6. Protein N-acetylglucosamine-6-phosphate deacetylase, NagA [82228] (3 species)

7. Species Escherichia coli [TaxId:562] [141688] (4 PDB entries)
   Uniprot P0AF18 1-53,351-382

8. Domain d2p50c1: 2p50 C:1-53,C:351-382 [149227]
   Other proteins in same PDB: d2p50a2, d2p50b2, d2p50c2, d2p50d2
   automatically matched to d1ymya1
   complexed with zn

Details for d2p50c1

PDB Entry: 2p50, 2.2 Å

PDB Description: Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn

PDB Compounds: (C:) N-acetylglucosamine-6-phosphate deacetylase

SCOP Domain Sequences for d2p50c1:

Sequence; same for both SEQRES and ATOM records:

>d2p50c1 b.92.1.5 (C:1-53,C:351-382) N-acetylglucosamine-6-phosphate deacetylase, NagA {Escherichia coli [TaxId: 562]}
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vanltaftpdfkitktivngnevvtq

Timeline for d2p50c1:

• d2p50c1 is new in SCOP 1.75
  
• d2p50c1 appears in SCOPe 2.01
  
• d2p50c1 appears in the current release, SCOPe 2.08