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Go to PDB code:
Transferase
PDB id
1ex0
Contents
Protein chains
705 a.a.
*
Ligands
PO4
×3
PGO
×6
Metals
_CA
×2
Waters
×1306
*
Residue conservation analysis
PDB id:
1ex0
Links
PDBe
RCSB
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
CSA
PROCOGNATE
ProSAT
EDS
Sacch3D
Whatcheck
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
Headers
References
Protein chains
?
P00488
(F13A_HUMAN) - Coagulation factor XIII A chain
Seq:
Struc:
 
Seq:
Struc:
732 a.a.
705 a.a.
*
Key:
PfamA 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 N
5
-alkylglutamine + NH
3
Protein glutamine
+
alkylamine
=
protein N(5)-alkylglutamine
+
NH(3)
Cofactor:
Calcium
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Gene Ontology (GO) functional annotation
Cellular component
extracellular region
3 terms
Biological process
wound healing
5 terms
Biochemical function
transferase activity
4 terms