Structure of PDB 3ghg Chain I Binding Site BS02

Receptor Information
>3ghg Chain I (length=394) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVE
NKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASIL
THDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGK
DCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGS
VDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELE
DWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSD
KFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQG
GTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIG
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 chain3ghg Chain I Residue 601 [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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PDB3ghg Crystal structure of human fibrinogen.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		D318 D320 F322 E323 G324
Binding residue
(residue number reindexed from 1)		D317 D319 F321 E322 G323
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:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0050839 cell adhesion molecule binding
Biological Process
GO:0007160 cell-matrix adhesion
GO:0007596 blood coagulation
GO:0009306 protein secretion
GO:0030168 platelet activation
GO:0031639 plasminogen activation
GO:0034116 positive regulation of heterotypic cell-cell adhesion
GO:0036345 platelet maturation
GO:0042730 fibrinolysis
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:0071354 cellular response to interleukin-6
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:0005788 endoplasmic reticulum lumen
GO:0005886 plasma membrane
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0031091 platelet alpha granule
GO:0031093 platelet alpha granule lumen
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:0072562 blood microparticle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ghg, PDBe:3ghg, PDBj:3ghg
PDBsum3ghg
PubMed19296670
UniProtP02679|FIBG_HUMAN Fibrinogen gamma chain (Gene Name=FGG)

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