Crystal structure of human Activated Protein C (APC) complexed with PPACK

Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human activated protein C (APC).

The 2.8 A crystal structure of Gla-domainless activated protein C.

THE NE2 HIS H - C3 0G6 AND OG SER H 195 - C2 0G7 BONDS ARE OUTSIDE ACCEPTED RANGE

Vitamin K-dependent protein C heavy chain

Vitamin K-dependent protein C light chain

Autoprothrombin IIA, Anticoagulant protein C, Blood coagulation factor XIV

LIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNY
SKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHN
ECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRD

QCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGD
DLLQCHPAVKFPCGRPWK

AUTHORS USED THE SF DATA FROM ENTRY 1AUT.

THE 2.8 A CRYSTAL STRUCTURE OF GLA-DOMAINLESS ACTIVATED PROTEIN C. Original refinement based on same data and R-free set.

THIS ENTRY 3F6U REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA R1AUTSF DETERMINED BY AUTHORS OF THE PDB ENTRY 1AUT: AUTHOR T.MATHER,V.OGANESSYAN,P.HOF,W.BODE,R.HUBER,S.FOUNDLING,C.ESMON

AUTHOR USED THE SF DATA FROM ENTRY 1AUT.

THE INHIBITOR IS BOUND TO THE ACTIVE SITE OF THE ENZYME. THE UNBOUND FORM OF THE INHIBITOR IS D-PHE-PRO-ARG-CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN IT FORMS TWO COVALENT BONDS: 1) A COVALENT BOND TO SER 195 FORMING A HEMIKETAL AR7 AND 2) A COVALENT BOND TO NE2 OF HIS 57

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

BLOOD COAGULATION, Serine protease, HYDROLASE-HYDROLASE INHIBITOR complex