Structure of PDB 2bq7 Chain B

Receptor sequence
>2bq7B (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB2bq7 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
Resolution2.2 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 IID B T98 Y99 R143 F174 D189 A190 C191 Q192 W215 G216 G219 T84 Y85 R132 F162 D179 A180 C181 Q182 W205 G206 G208 PDBbind-CN: -logKd/Ki=7.05,Ki=89nM
BindingDB: Ki=89nM
BS02 CA B D70 N72 Q75 E76 E80 D56 N58 Q61 E62 E66
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2bq7, PDBe:2bq7, PDBj:2bq7
PDBsum2bq7
PubMed15999990
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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