1RFN

HUMAN COAGULATION FACTOR IXA IN COMPLEX WITH P-AMINO BENZAMIDINE

Summary for 1RFN

• Entry DOI: 10.2210/pdb1rfn/pdb
• Descriptor: PROTEIN (COAGULATION FACTOR IX), CALCIUM ION, P-AMINO BENZAMIDINE, ... (6 entities in total)
• Functional Keywords: serine proteinase, blood coagulation, coagulation factor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P00740 P00740
• Total number of polymer chains: 2
• Total formula weight: 32697.33

Authors

Hopfner, K.-P.,Lang, A.,Karcher, A.,Sichler, K.,Kopetzki, E.,Brandstetter, H.,Huber, R.,Bode, W.,Engh, R.A. (deposition date: 1999-04-19, release date: 1999-09-01, Last modification date: 2024-10-16)

Primary citation

Hopfner, K.P.,Lang, A.,Karcher, A.,Sichler, K.,Kopetzki, E.,Brandstetter, H.,Huber, R.,Bode, W.,Engh, R.A.
Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.
Structure Fold.Des., 7:989-996, 1999

PubMed Abstract: Among the S1 family of serine proteinases, the blood coagulation factor IXa (fIXa) is uniquely inefficient against synthetic peptide substrates. Mutagenesis studies show that a loop of residues at the S2-S4 substrate-binding cleft (the 99-loop) contributes to the low efficiency. The crystal structure of porcine fIXa in complex with the inhibitor D-Phe-Pro-Arg-chloromethylketone (PPACK) was unable to directly clarify the role of the 99-loop, as the doubly covalent inhibitor induced an active conformation of fIXa.

PubMed: 10467148
DOI: 10.1016/S0969-2126(99)80125-7

Experimental method

X-RAY DIFFRACTION (2.8 Å)