Structure of PDB 2h43 Chain E Binding Site BS02

Receptor Information
>2h43 Chain E (length=302) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVV
SGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQ
DGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMG
PTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDG
ASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNR
CHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRP
FF
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2h43 Chain E Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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.
Resolution2.7 Å
Binding residue
(original residue number in PDB)
D381 D383 W385
Binding residue
(residue number reindexed from 1)
D225 D227 W229
Annotation score4
Enzymatic activity
Enzyme Commision number ?
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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