SCOP 1.75: Domain d1o9sb2: 1o9s B:194-366

Lineage for d1o9sb2 (1o9s B:194-366)

1. Root: SCOP 1.75

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

3. Fold b.85: beta-clip [51268] (7 superfamilies)
   double-stranded ribbon sharply bent in two places; the ribbon ends form incomplete barrel; jelly-roll

4. Superfamily b.85.7: SET domain [82199] (3 families)
   duplication: the core is composed of two structural repeats similar to (circularly permuted) repeats of AFPIII
   also contains a substrate-binding alpha+beta subdomain inserted in the core

5. Family b.85.7.1: Histone lysine methyltransferases [82200] (3 proteins)
   contains metal-binding preSET and postSET domains

6. Protein Histone H3 K4-specific methyltransferase SET7/9 catalytic domain [82205] (1 species)

7. Species Human (Homo sapiens) [TaxId:9606] [82206] (11 PDB entries)
   Uniprot Q8WTS6 52-336

8. Domain d1o9sb2: 1o9s B:194-366 [81252]
   Other proteins in same PDB: d1o9sa1, d1o9sb1
   complexed with mlz, sah

Details for d1o9sb2

PDB Entry: 1o9s, 1.75 Å

PDB Description: crystal structure of a ternary complex of the human histone methyltransferase set7/9

PDB Compounds: (B:) histone-lysine n-methyltransferase, h3 lysine-4 specific

SCOP Domain Sequences for d1o9sb2:

Sequence; same for both SEQRES and ATOM records:

>d1o9sb2 b.85.7.1 (B:194-366) Histone H3 K4-specific methyltransferase SET7/9 catalytic domain {Human (Homo sapiens) [TaxId: 9606]}
dkstsscistnallpdpyeservyvaeslissageglfskvavgpntvmsfyngvrithq
evdsrdwalngntlsldeetvidvpepynhvskycaslghkanhsftpnciydmfvhprf
gpikcirtlraveadeeltvaygydhsppgksgpeapewyqvelkafqatqqk

Timeline for d1o9sb2:

• d1o9sb2 first appeared in SCOP 1.63
  
• d1o9sb2 appears in SCOP 1.73
  
• d1o9sb2 appears in SCOPe 2.01
  
• d1o9sb2 appears in the current release, SCOPe 2.08