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PDBsum entry 1ex0
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Tryptophan 279 is essential for the transglutaminase activity of coagulation factor xiii: functional and structural characterization
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Authors
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R.J.Garzon,
K.P.Pratt,
P.D.Bishop,
I.Le trong,
R.E.Stenkamp,
D.C.Teller.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor xiii by x-Ray crystallography.
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Authors
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B.A.Fox,
V.C.Yee,
L.C.Pedersen,
I.Le trong,
P.D.Bishop,
R.E.Stenkamp,
D.C.Teller.
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Ref.
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J Biol Chem, 1999,
274,
4917-4923.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Overall structure of the factor XIII dimer. Panel
A is the dimer looking down the two-fold axis. The domains,
activation peptide (AP), and N and C termini of one monomer are
labeled. Panel B shows one monomer, rotated 90° with the
domains, N terminus, active site (AS), and ion sites labeled.
For both views, three unique spheres are also shown: novel
ytterbium site on the dimer two-fold axis (medium gray), active
site (light gray), and main ion site (dark gray).
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Figure 6.
Fig. 6. Structurally significant water molecule. Water
6059S is shown as a sphere with several secondary structure
elements nearby. The residues near this water are also shown.
The active site residue His-373 and calcium binding ligand
Ala-457 are shown.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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