Structure of PDB 2vh0 Chain A

Receptor sequence
>2vh0A (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB2vh0 Structure and property based design of factor Xa inhibitors: biaryl pyrrolidin-2-ones incorporating basic heterocyclic motifs.
ChainA
Resolution1.7 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 A D70 N72 Q75 E80 D56 N58 Q61 E66
BS02 MG A Y185 D185A R222 K224 Y173 D174 R211 K214
BS03 GSI A K96 E97 T98 Y99 F174 D189 A190 Q192 V213 W215 G216 G226 I227 Y228 K82 E83 T84 Y85 F162 D179 A180 Q182 V203 W205 G206 G216 I217 Y218 MOAD: Ki<1nM
PDBbind-CN: -logKd/Ki=8.51,Ki=3.1nM
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:2vh0, PDBe:2vh0, PDBj:2vh0
PDBsum2vh0
PubMed18053714
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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