1DUG

STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION

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Functional Information from GO Data

ChainGOidnamespacecontents
A0072562cellular_componentblood microparticle
A0009986cellular_componentcell surface
A0062023cellular_componentcollagen-containing extracellular matrix
A0005788cellular_componentendoplasmic reticulum lumen
A0009897cellular_componentexternal side of plasma membrane
A0070062cellular_componentextracellular exosome
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005577cellular_componentfibrinogen complex
A0005886cellular_componentplasma membrane
A0031091cellular_componentplatelet alpha granule
A0031093cellular_componentplatelet alpha granule lumen
A0050839molecular_functioncell adhesion molecule binding
A0005201molecular_functionextracellular matrix structural constituent
A0046872molecular_functionmetal ion binding
A0042803molecular_functionprotein homodimerization activity
A0005102molecular_functionsignaling receptor binding
A0005198molecular_functionstructural molecule activity
A0007596biological_processblood coagulation
A0072378biological_processblood coagulation, fibrin clot formation
A0007160biological_processcell-matrix adhesion
A0044267biological_processcellular protein metabolic process
A0034622biological_processcellular protein-containing complex assembly
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0030198biological_processextracellular matrix organization
A0042730biological_processfibrinolysis
A2000352biological_processnegative regulation of endothelial cell apoptotic process
A1902042biological_processnegative regulation of extrinsic apoptotic signaling pathway via death domain receptors
A0090331biological_processnegative regulation of platelet aggregation
A0031639biological_processplasminogen activation
A0070527biological_processplatelet aggregation
A0002576biological_processplatelet degranulation
A0036345biological_processplatelet maturation
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0045921biological_processpositive regulation of exocytosis
A0034116biological_processpositive regulation of heterotypic cell-cell adhesion
A0090277biological_processpositive regulation of peptide hormone secretion
A0050714biological_processpositive regulation of protein secretion
A1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
A0045907biological_processpositive regulation of vasoconstriction
A0043687biological_processpost-translational protein modification
A0051258biological_processprotein polymerization
A0009306biological_processprotein secretion
A0051592biological_processresponse to calcium ion
A0002224biological_processtoll-like receptor signaling pathway
B0072562cellular_componentblood microparticle
B0009986cellular_componentcell surface
B0062023cellular_componentcollagen-containing extracellular matrix
B0005788cellular_componentendoplasmic reticulum lumen
B0009897cellular_componentexternal side of plasma membrane
B0070062cellular_componentextracellular exosome
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005577cellular_componentfibrinogen complex
B0005886cellular_componentplasma membrane
B0031091cellular_componentplatelet alpha granule
B0031093cellular_componentplatelet alpha granule lumen
B0050839molecular_functioncell adhesion molecule binding
B0005201molecular_functionextracellular matrix structural constituent
B0046872molecular_functionmetal ion binding
B0042803molecular_functionprotein homodimerization activity
B0005102molecular_functionsignaling receptor binding
B0005198molecular_functionstructural molecule activity
B0007596biological_processblood coagulation
B0072378biological_processblood coagulation, fibrin clot formation
B0007160biological_processcell-matrix adhesion
B0044267biological_processcellular protein metabolic process
B0034622biological_processcellular protein-containing complex assembly
B0071347biological_processcellular response to interleukin-1
B0071354biological_processcellular response to interleukin-6
B0030198biological_processextracellular matrix organization
B0042730biological_processfibrinolysis
B2000352biological_processnegative regulation of endothelial cell apoptotic process
B1902042biological_processnegative regulation of extrinsic apoptotic signaling pathway via death domain receptors
B0090331biological_processnegative regulation of platelet aggregation
B0031639biological_processplasminogen activation
B0070527biological_processplatelet aggregation
B0002576biological_processplatelet degranulation
B0036345biological_processplatelet maturation
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0045921biological_processpositive regulation of exocytosis
B0034116biological_processpositive regulation of heterotypic cell-cell adhesion
B0090277biological_processpositive regulation of peptide hormone secretion
B0050714biological_processpositive regulation of protein secretion
B1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
B0045907biological_processpositive regulation of vasoconstriction
B0043687biological_processpost-translational protein modification
B0051258biological_processprotein polymerization
B0009306biological_processprotein secretion
B0051592biological_processresponse to calcium ion
B0002224biological_processtoll-like receptor signaling pathway
A0004364molecular_functionglutathione transferase activity
B0004364molecular_functionglutathione transferase activity
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC120BINDING SITE FOR RESIDUE GSH A 1239
ChainResidue
ATYR6
ATRP7
ALEU12
ATRP40
ALYS44
AASN53
ALEU54
APRO55
AGLN66
ASER67
AHOH1243
AHOH1244
AHOH1258
AHOH1352
AHOH1363
AHOH1529
AHOH1545
BASP100
BHOH1689
BHOH1711

AC219BINDING SITE FOR RESIDUE GSH B 1587
ChainResidue
AASP100
AHOH1249
BTYR6
BTRP7
BLEU12
BTRP40
BLYS44
BASN53
BLEU54
BPRO55
BGLN66
BSER67
BHOH1588
BHOH1590
BHOH1605
BHOH1728
BHOH1829
BHOH1833
BHOH1840

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
GSH_1dug_A_123914GLUTATHIONE binding site
ChainResidueligand
ATYR6-TRP7GSH: GLUTATHIONE
ALEU12GSH: GLUTATHIONE
ATRP40GSH: GLUTATHIONE
ALYS44GSH: GLUTATHIONE
AASN53-PRO55GSH: GLUTATHIONE
AGLN66-MET68GSH: GLUTATHIONE
ATYR103GSH: GLUTATHIONE
BGLY96GSH: GLUTATHIONE
BASP100GSH: GLUTATHIONE

GSH_1dug_B_158714GLUTATHIONE binding site
ChainResidueligand
AGLY96GSH: GLUTATHIONE
AASP100GSH: GLUTATHIONE
BTYR6-TRP7GSH: GLUTATHIONE
BLEU12GSH: GLUTATHIONE
BTRP40GSH: GLUTATHIONE
BLYS44GSH: GLUTATHIONE
BASN53-PRO55GSH: GLUTATHIONE
BGLN66-MET68GSH: GLUTATHIONE
BTYR103GSH: GLUTATHIONE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI12Calcium. {ECO:0000244|PDB:1FID, ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719, ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}
ChainResidueDetails
ANA*
ANA*

SWS_FT_FI22Calcium; via carbonyl oxygen. {ECO:0000244|PDB:1FID, ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719, ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}
ChainResidueDetails
ANA*
ANA*

SWS_FT_FI34Cleavage; by plasmin; to break down fibrin clots.
ChainResidueDetails
ANA*
ANA*

SWS_FT_FI42Cleavage; by hementin; to prevent blood coagulation.
ChainResidueDetails
ANA*

SWS_FT_FI52Calcium. {ECO:0000244|PDB:1FID, ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719, ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}
ChainResidueDetails
BNA*
BNA*

SWS_FT_FI62Calcium; via carbonyl oxygen. {ECO:0000244|PDB:1FID, ECO:0000269|PubMed:10074346, ECO:0000269|PubMed:19296670, ECO:0000269|PubMed:9016719, ECO:0000269|PubMed:9207064, ECO:0000269|PubMed:9333233, ECO:0000269|PubMed:9628725}
ChainResidueDetails
BNA*
BNA*

SWS_FT_FI74Cleavage; by plasmin; to break down fibrin clots.
ChainResidueDetails
BNA*
BNA*

SWS_FT_FI82Cleavage; by hementin; to prevent blood coagulation.
ChainResidueDetails
BNA*

CSA11Annotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR6

CSA21Annotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR6

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA11Annotated By Reference To The Literature 1oe8
ChainResidueDetails
ATYR6

CSA21Annotated By Reference To The Literature 1oe8
ChainResidueDetails
BTYR6