spacer
spacer

PDBsum entry 4e2f

Go to PDB code: 
protein metals Protein-protein interface(s) links
Transferase/protein binding PDB id
4e2f

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
(+ 0 more) 310 a.a.
(+ 0 more) 144 a.a.
Metals
_ZN ×6
Waters ×506
PDB id:
4e2f
Name: Transferase/protein binding
Title: Crystal structure of e. Coli aspartate transcarbamoylase k164e/e239k mutant in an intermediate state
Structure: Aspartate carbamoyltransferase catalytic chain. Chain: i, k, g, c, a, e. Synonym: aspartate transcarbamylase, atcase. Engineered: yes. Mutation: yes. Aspartate carbamoyltransferase regulatory chain. Chain: d, b, j, l, h, f. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b4245, jw4204, pyrb. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b4244, jw4203, pyri.
Resolution:
2.80Å     R-factor:   0.217     R-free:   0.274
Authors: W.Guo,E.R.Kantrowitz
Key ref: W.Guo et al. (2012). Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase. Proc Natl Acad Sci U S A, 109, 7741-7746. PubMed id: 22547808
Date:
08-Mar-12     Release date:   02-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A786  (PYRB_ECOLI) -  Aspartate carbamoyltransferase catalytic subunit from Escherichia coli (strain K12)
Seq:
Struc:
311 a.a.
310 a.a.*
Protein chains
Pfam   ArchSchema ?
P0A7F3  (PYRI_ECOLI) -  Aspartate carbamoyltransferase regulatory chain from Escherichia coli (strain K12)
Seq:
Struc:
153 a.a.
144 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains I, K, G, C, A, E: E.C.2.1.3.2  - aspartate carbamoyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Pyrimidine Biosynthesis
      Reaction: carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H+
carbamoyl phosphate
+ L-aspartate
= N-carbamoyl-L-aspartate
+ phosphate
+ H(+)
   Enzyme class 3: Chains D, B, J, L, H, F: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 109:7741-7746 (2012)
PubMed id: 22547808  
 
 
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.
W.Guo, J.M.West, A.S.Dutton, H.Tsuruta, E.R.Kantrowitz.
 
  ABSTRACT  
 
No abstract given.

 

 

spacer

spacer