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PDBsum entry 3ttc

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protein ligands metals links
Transferase PDB id
3ttc

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
646 a.a.
Ligands
ADP ×2
Metals
_ZN ×3
_MG
Waters ×918
PDB id:
3ttc
Name: Transferase
Title: Crystal structure of e. Coli hypf with adp and carbamoyl phosphate
Structure: Transcriptional regulatory protein. Chain: a. Fragment: unp residues 92-746. Synonym: hypf. Engineered: yes
Source: Escherichia coli. Organism_taxid: 83334. Strain: o157. Gene: ecs3568, hypf. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.86Å     R-factor:   0.161     R-free:   0.202
Authors: S.Petkun,R.Shi,Y.Li,M.Cygler
Key ref: S.Petkun et al. (2011). Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites. Structure, 19, 1773-1783. PubMed id: 22153500
Date:
14-Sep-11     Release date:   28-Dec-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
A0A0H3JHT3  (A0A0H3JHT3_ECO57) -  Carbamoyltransferase HypF from Escherichia coli O157:H7
Seq:
Struc:
 
Seq:
Struc:
750 a.a.
646 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: E.C.3.6.1.7  - acylphosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: an acyl phosphate + H2O = a carboxylate + phosphate + H+
acyl phosphate
+ H2O
= carboxylate
+ phosphate
+ H(+)
   Enzyme class 3: E.C.6.2.-.-
[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    
 
 
Structure 19:1773-1783 (2011)
PubMed id: 22153500  
 
 
Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites.
S.Petkun, R.Shi, Y.Li, A.Asinas, C.Munger, L.Zhang, M.Waclawek, B.Soboh, R.G.Sawers, M.Cygler.
 
  ABSTRACT  
 
No abstract given.

 

 

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