Structure of PDB 2h43 Chain E

Receptor sequence
>2h43E (length=302) Species: 9606 (Homo sapiens) [Search protein sequence]
VNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVV
SGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQ
DGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMG
PTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDG
ASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNR
CHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRP
FF
3D structure
PDB2h43 Differences in Binding Specificity for the Homologous gamma- and beta-Chain "Holes" on Fibrinogen: Exclusive Binding of Ala-His-Arg-Pro-amide by the beta-Chain Hole.
ChainE
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 peptide E N364 M367 W385 E397 R406 C407 H408 D432 N208 M211 W229 E241 R250 C251 H252 D276
BS02 CA E D381 D383 W385 D225 D227 W229
Gene Ontology
Molecular Function
GO:0005102 signaling receptor binding
Biological Process
GO:0007596 blood coagulation
GO:0030168 platelet activation
GO:0051258 protein polymerization
Cellular Component
GO:0005577 fibrinogen complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2h43, PDBe:2h43, PDBj:2h43
PDBsum2h43
PubMed17115691
UniProtP02675|FIBB_HUMAN Fibrinogen beta chain (Gene Name=FGB)

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