Structure of PDB 2pr3 Chain A

Receptor sequence
>2pr3A (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB2pr3 Structure-based drug design of pyrrolidine-1, 2-dicarboxamides as a novel series of orally bioavailable factor Xa inhibitors
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H42 D88 Q182 G183 D184 S185 G186
Enzyme Commision number 3.4.21.6: coagulation factor Xa.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A D70 N72 Q75 E80 D56 N58 Q61 E66
BS02 CA A Y185 D185A R222 K224 Y173 D174 R211 K214
BS03 237 A E97 T98 Y99 F174 A190 C191 V213 W215 G216 G219 C220 G226 I227 Y228 E83 T84 Y85 F162 A180 C181 V203 W205 G206 G208 C209 G216 I217 Y218 MOAD: ic50=0.16nM
BindingDB: IC50=0.16nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:2pr3, PDBe:2pr3, PDBj:2pr3
PDBsum2pr3
PubMed17581239
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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