PDBsum entry 1evu

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Transferase PDB id
Protein chain
708 a.a. *
_CA ×2
Waters ×1159
* Residue conservation analysis

References listed in PDB file
Key reference
Title Tryptophan 279 is essential for the transglutaminase activity of coagulation factor xiii: functional and structural characterization
Authors R.J.Garzon, K.P.Pratt, P.D.Bishop, I.Le trong, R.E.Stenkamp, D.C.Teller.
Ref. To Be Published ...
Secondary reference #1
Title Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor xiii by x-Ray crystallography.
Authors B.A.Fox, V.C.Yee, L.C.Pedersen, I.Le trong, P.D.Bishop, R.E.Stenkamp, D.C.Teller.
Ref. J Biol Chem, 1999, 274, 4917-4923. [DOI no: 10.1074/jbc.274.8.4917]
PubMed id 9988734
Full text Abstract
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).
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.
The above figures are reproduced from the cited reference with permission from the ASBMB
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