Structural Classification of Proteins
home mail help root up expand collapse

Protein: Glycinamide ribonucleotide transformylase PurT, domain 2 from Escherichia coli [TaxId: 562]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: ATP-grasp [56058]
    Consists of two subdomains with different alpha+beta folds
    shares functional and structural similarities with the PIPK and protein kinase superfamilies
  4. Superfamily: Glutathione synthetase ATP-binding domain-like [56059]
    link to SUPERFAMILY database - Superfamily
  5. Family: BC ATP-binding domain-like [56067]
  6. Protein: Glycinamide ribonucleotide transformylase PurT, domain 2 [56074]
  7. Species: Escherichia coli [TaxId: 562] [56075]

PDB Entry Domains:

  1. 1kjq picpicxrefxref
    complexed with adp, cl, edo, mg, mpo, na
    1. region a:113-318 [72618] picpiclink
    2. region b:113-318 [72621] picpiclink
  2. 1kj9 picpicxrefxref
    complexed with atp, cl, edo, mg, mpo, na
    1. region a:113-318 [72591] picpiclink
    2. region b:113-318 [72594] picpiclink
  3. 1kj8 picpicxrefxref
    complexed with atp, cl, edo, gar, mg, mpo, na
    1. region a:113-318 [72585] picpiclink
    2. region b:113-318 [72588] picpiclink
  4. 1kji picpicxrefxref
    complexed with acp, cl, edo, mg, mpo, na
    1. region a:113-318 [72603] picpiclink
    2. region b:113-318 [72606] picpiclink
  5. 1kjj picpicxrefxref
    complexed with ags, cl, mg, mpo, na
    1. region a:113-318 [72609] picpiclink
    2. region b:113-318 [72612] picpiclink
  6. 1ez1 picpicxrefxref
    complexed with act, anp, gar, mg, mpo, na
    1. region a:113-318 [41500] picpiclink
    2. region b:113-318 [41501] picpiclink
  7. 1eyz picpicxrefxref
    complexed with anp, cl, mg, mpo, na
    1. region a:113-318 [41498] picpiclink
    2. region b:113-318 [41499] picpiclink
Enter search key:
MRC site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk