Structure of PDB 1nfu Chain A

Receptor sequence
>1nfuA (length=234) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRF
KVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITF
RMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPY
VDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVT
GIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKT
3D structure
PDB1nfu Molecular structures of human Factor Xa complexed with ketopiperazine inhibitors: preference for a neutral group in the S1 pocket.
ChainA
Resolution2.05 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 RRP A F174 D189 A190 C191 Q192 V213 W215 G216 E217 G219 C220 G226 I227 Y228 F162 D179 A180 C181 Q182 V203 W205 G206 E207 G208 C209 G216 I217 Y218 MOAD: Ki=18nM
PDBbind-CN: -logKd/Ki=7.74,Ki=18nM
BindingDB: Ki=4nM
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:1nfu, PDBe:1nfu, PDBj:1nfu
PDBsum1nfu
PubMed12593649
UniProtP00742|FA10_HUMAN Coagulation factor X (Gene Name=F10)

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