Structure of PDB 3ghg Chain B Binding Site BS01

Receptor Information

>3ghg Chain B (length=401) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

KAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAV
SQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETV
NSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVS
GKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQD
GSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGP
TELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGA
SQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRC
HAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPF
F

Ligand information

>3ghg Chain O (length=4) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

GHRP

Receptor-Ligand Complex Structure

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Structure summary

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PDB	3ghg Crystal structure of human fibrinogen.
Resolution	2.9 Å
Binding residue (original residue number in PDB)	L360 N364 M367 W385 E397 D398 R406 C407 H408 T431 D432 M438
Binding residue (residue number reindexed from 1)	L303 N307 M310 W328 E340 D341 R349 C350 H351 T374 D375 M381

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

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3ghg, PDBe:3ghg, PDBj:3ghg
PDBsum	3ghg
PubMed	19296670
UniProt	P02675\|FIBB_HUMAN Fibrinogen beta chain (Gene Name=FGB)

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