SCOP 1.73: Domain d1opma2: 1opm A:199-354

Lineage for d1opma2 (1opm A:199-354)

1. Root: SCOP 1.73

2. Class b: All beta proteins [48724] (165 folds)

3. Fold b.121: Nucleoplasmin-like/VP (viral coat and capsid proteins) [88632] (7 superfamilies)
   sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands
   characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies

4. Superfamily b.121.1: PHM/PNGase F [49742] (2 families)
   members of this superfamily bind peptide substrates
   duplication: consists of two domains of this fold packed together like the adjacent nucleoplasmin subunits

5. Family b.121.1.2: Peptidylglycine alpha-hydroxylating monooxygenase, PHM [49746] (1 protein)

6. Protein Peptidylglycine alpha-hydroxylating monooxygenase, PHM [63402] (1 species)

7. Species Rat (Rattus norvegicus) [TaxId:10116] [49748] (8 PDB entries)

8. Domain d1opma2: 1opm A:199-354 [59014]
   complexed with 1cu, azi, cu, gol, iyg, ni1

Details for d1opma2

PDB Entry: 1opm, 2.1 Å

PDB Description: oxidized (cu2+) peptidylglycine alpha-hydroxylating monooxygenase (phm) with bound substrate

PDB Compounds: (A:) protein (peptidylglycine alpha-hydroxylating monooxygenase)

SCOP Domain Sequences for d1opma2:

Sequence; same for both SEQRES and ATOM records:

>d1opma2 b.121.1.2 (A:199-354) Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Rat (Rattus norvegicus) [TaxId: 10116]}
pliagmylmmsvdtvippgekvvnadiscqykmypmhvfayrvhthhlgkvvsgyrvrng
qwtligrqnpqlpqafypvehpvdvtfgdilaarcvftgegrteathiggtssdemcnly
imyymeakyalsfmtctknvapdmfrtipaeanipi

Timeline for d1opma2:

• d1opma2 first appeared in SCOP 1.57
  
• d1opma2 appears in SCOP 1.71
  
• d1opma2 appears in SCOP 1.75
  
• d1opma2 appears in the current release, SCOPe 2.08