SCOP 1.75: Domain d2ofjd1: 2ofj D:100-320

Lineage for d2ofjd1 (2ofj D:100-320)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.11: Enolase C-terminal domain-like [51604] (2 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this superfamily

5. Family c.1.11.2: D-glucarate dehydratase-like [51609] (13 proteins)

6. Protein O-succinylbenzoate synthase [51613] (1 species)

7. Species Escherichia coli [TaxId:562] [51614] (4 PDB entries)

8. Domain d2ofjd1: 2ofj D:100-320 [139050]
   Other proteins in same PDB: d2ofja2, d2ofjb2, d2ofjc2, d2ofjd2
   automatically matched to d1fhua1
   mutant

Details for d2ofjd1

PDB Entry: 2ofj, 2.3 Å

PDB Description: crystal structure of the e190a mutant of o-succinylbenzoate synthase from escherichia coli

PDB Compounds: (D:) o-succinylbenzoate synthase

SCOP Domain Sequences for d2ofjd1:

Sequence, based on SEQRES records:

>d2ofjd1 c.1.11.2 (D:100-320) O-succinylbenzoate synthase {Escherichia coli [TaxId: 562]}
qaanyraaplcngdpddlilkladmpgekvakvkvglyeavrdgmvvnllleaipdlhlr
ldanrawtplkgqqfakyvnpdyrdriaflaepcktrddsrafaretgiaiawdeslrep
dfafvaeegvravvikptltgslekvreqvqaahalgltavisssiesslgltqlariaa
wltpdtipgldtldlmqaqqvrrwpgstlpvvevdalerll

Sequence, based on observed residues (ATOM records):

>d2ofjd1 c.1.11.2 (D:100-320) O-succinylbenzoate synthase {Escherichia coli [TaxId: 562]}
qaanyraaplcngdpekvakvkvglyeavrdgmvvnllleaipdlhlrldanrawtplkg
qqfakyvnpdyrdriaflaepcktrddsrafaretgiaiawdeslrepdfafvaeegvra
vvikptltgslekvreqvqaahalgltavisssiesslgltqlariaawltpdtipgldt
ldlmqaqqvrrwpgstlpvvevdalerll

Timeline for d2ofjd1:

• d2ofjd1 first appeared in SCOP 1.73
  
• d2ofjd1 appears in SCOPe 2.01
  
• d2ofjd1 appears in the current release, SCOPe 2.08