1KIG
BOVINE FACTOR XA
Summary for 1KIG
| Entry DOI | 10.2210/pdb1kig/pdb |
| Descriptor | FACTOR XA, ANTICOAGULANT PEPTIDE (3 entities in total) |
| Functional Keywords | glycoprotein, serine protease, plasma, blood coagulation, complex (protease-inhibitor), complex (protease-inhibitor) complex, complex (protease/inhibitor) |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Secreted: P00743 P00743 |
| Total number of polymer chains | 3 |
| Total formula weight | 39473.39 |
| Authors | Wei, A.,Alexander, R.,Chang, C.-H. (deposition date: 1997-04-24, release date: 1998-10-28, Last modification date: 2024-10-23) |
| Primary citation | Wei, A.,Alexander, R.S.,Duke, J.,Ross, H.,Rosenfeld, S.A.,Chang, C.H. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J.Mol.Biol., 283:147-154, 1998 Cited by PubMed Abstract: The structure of recombinant tick anticoagulant peptide (rTAP) complexed to bovine factor Xa at 3.0 A resolution reveals the structural basis for the specificity and the high affinity of rTAP. Three N-terminal residues, Tyr501, Asn502 and Arg503, play a critical role in the complex formation as suggested by earlier mutagenic studies and the ornithodorin-thrombin complex. Unexpectedly, the side-chain of Tyr501 is located in the S1 pocket, although factor Xa favors arginine as a P1 residue. Arg503 is located at the aryl binding pocket and forms a salt-bridge with Glu97 of factor Xa. The autolysis loop, which is disordered in the uninhibited factor Xa structure, is involved in the formation of the complex as a part of the secondary binding site. The C-terminal helix of rTAP interacts with factor Xa as a secondary binding determinant. The N-terminal residues of rTAP reorganize during the formation of the factor Xa-rTAP complex from the conformation found in the solution into an extended conformation. The presence of the secondary binding site confirms the proposed two-step kinetic mechanism based on the results of a mutagenesis study. PubMed: 9761680DOI: 10.1006/jmbi.1998.2069 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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