PDBsum entry 1ex0

Transferase

PDB id

1ex0

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Contents

			Protein chain

					705 a.a. *

			Ligands

					PO4 ×3


					PGO ×6

			Metals

					_CA ×2

			Waters ×1306

* Residue conservation analysis

PDB id:

1ex0

Links

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 from Homo sapiens

Seq: Struc:

Seq: Struc:					732 a.a. 705 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 2 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.2.3.2.13 - protein-glutamine gamma-glutamyltransferase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N₆-5- L-glutamyl-[protein] + NH4⁺

protein-L-glutamine	+	protein-L-lysine	=	protein with an N(6)- (gamma-glutamyl)-L-lysine cross-link	+	NH(3)

Cofactor:

Ca(2+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site