Structure of PDB 2bmg Chain B

Receptor sequence
>2bmgB (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB2bmg Structural Requirements for Factor Xa Inhibition by 3-Oxybenzamides with Neutral P1 Substituents: Combining X-Ray Crystallography, 3D-Qsar and Tailored Scoring Functions
ChainB
Resolution2.7 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 E77 E80 D56 N58 Q61 E62 E63 E66
BS02 I1H B T98 Y99 F174 D189 A190 C191 W215 G216 G219 C220 G226 I227 Y228 T84 Y85 F162 D179 A180 C181 W205 G206 G208 C209 G216 I217 Y218 PDBbind-CN: -logKd/Ki=7.74,Ki=18nM
BindingDB: Ki=18nM
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:2bmg, PDBe:2bmg, PDBj:2bmg
PDBsum2bmg
PubMed15857135
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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