Structure of PDB 2bq6 Chain B

Receptor sequence
>2bq6B (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB2bq6 Probing the Subpockets of Factor Xa Reveals Two Binding Modes for Inhibitors Based on a 2-Carboxyindole Scaffold: A Study Combining Structure-Activity Relationship and X-Ray Crystallography.
ChainB
Resolution3.0 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 B D70 N72 Q75 E76 E80 D56 N58 Q61 E62 E66
BS02 IIB B Y99 E147 F174 D189 A190 C191 Q192 W215 G216 E217 G219 G226 Y228 Y85 E135 F162 D179 A180 C181 Q182 W205 G206 E207 G208 G216 Y218 PDBbind-CN: -logKd/Ki=10.15,Ki=0.07nM
BindingDB: Ki=0.07nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2bq6, PDBe:2bq6, PDBj:2bq6
PDBsum2bq6
PubMed15999990
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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