Structure of PDB 3h32 Chain B Binding Site BS02

Receptor Information
>3h32 Chain B (length=308) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVS
CNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWT
VIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKIS
QLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAG
NALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGG
GWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKM
SMKIRPFF
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 chain3h32 Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3h32 Two families of synthetic peptides that enhance fibrin turbidity and delay fibrinolysis by different mechanisms.
Resolution3.6 Å
Binding residue
(original residue number in PDB)		D381 D383 W385
Binding residue
(residue number reindexed from 1)		D231 D233 W235
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005102 signaling receptor binding
GO:0005198 structural molecule activity
GO:0005201 extracellular matrix structural constituent
GO:0005515 protein binding
GO:0050839 cell adhesion molecule binding
GO:0051087 protein-folding chaperone binding
Biological Process
GO:0002250 adaptive immune response
GO:0007160 cell-matrix adhesion
GO:0007596 blood coagulation
GO:0030168 platelet activation
GO:0031639 plasminogen activation
GO:0034116 positive regulation of heterotypic cell-cell adhesion
GO:0042730 fibrinolysis
GO:0043152 induction of bacterial agglutination
GO:0044320 cellular response to leptin stimulus
GO:0045087 innate immune response
GO:0045907 positive regulation of vasoconstriction
GO:0045921 positive regulation of exocytosis
GO:0050714 positive regulation of protein secretion
GO:0051258 protein polymerization
GO:0051592 response to calcium ion
GO:0065003 protein-containing complex assembly
GO:0070374 positive regulation of ERK1 and ERK2 cascade
GO:0070527 platelet aggregation
GO:0071347 cellular response to interleukin-1
GO:0072378 blood coagulation, fibrin clot formation
GO:0090277 positive regulation of peptide hormone secretion
GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
GO:1902042 negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
GO:2000352 negative regulation of endothelial cell apoptotic process
Cellular Component
GO:0005576 extracellular region
GO:0005577 fibrinogen complex
GO:0005615 extracellular space
GO:0005783 endoplasmic reticulum
GO:0005886 plasma membrane
GO:0005938 cell cortex
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0031091 platelet alpha granule
GO:0031093 platelet alpha granule lumen
GO:0045202 synapse
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:0072562 blood microparticle
GO:1903561 extracellular vesicle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3h32, PDBe:3h32, PDBj:3h32
PDBsum3h32
PubMed19588915
UniProtP02675|FIBB_HUMAN Fibrinogen beta chain (Gene Name=FGB)

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