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PDBsum entry 1ex0

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1ex0
Jmol
Contents
Protein chain
705 a.a. *
Ligands
PO4 ×3
PGO ×6
Metals
_CA ×2
Waters ×1306
* Residue conservation analysis
PDB id:
1ex0
Name: Transferase
Title: Human factor xiii, mutant w279f zymogen
Structure: Coagulation factor xiii a chain. Chain: a, b. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Biol. unit: Dimer (from PQS)
Resolution:
2.00Å     R-factor:   0.187     R-free:   0.234
Authors: R.J.Garzon,K.P.Pratt,P.D.Bishop,I.Le Trong,R.E.Stenkamp, D.C.Teller
Key ref: R.J.Garzon et al. Tryptophan 279 is essential for the transglutaminase activity of coagulation factor xiii: functional and structural characterization. To be published, .
Date:
28-Apr-00     Release date:   23-Dec-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00488  (F13A_HUMAN) -  Coagulation factor XIII A chain
Seq:
Struc:
 
Seq:
Struc:
732 a.a.
705 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.3.2.13  - Protein-glutamine gamma-glutamyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Protein glutamine
+ alkylamine
= protein N(5)-alkylglutamine
+ NH(3)
      Cofactor: Ca(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   4 terms 
  Biological process     hemostasis   5 terms 
  Biochemical function     transferase activity     4 terms