Structure of PDB 1m1j Chain E

Receptor sequence
>1m1jE (length=401) Species: 9031 (Gallus gallus) [Search protein sequence]
IYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKF
SDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNL
DNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVS
GRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQD
GSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPT
KVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGAS
QLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCH
AANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYF
P
3D structure
PDB1m1j Crystal Structure of Native Chicken Fibrinogen at 2.7 A Resolution
ChainE
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide E L364 M371 W389 E401 D402 R410 C411 H412 T435 D436 M442 L302 M309 W327 E339 D340 R348 C349 H350 T373 D374 M380
BS02 CA E D385 D387 W389 D323 D325 W327
Gene Ontology
Molecular Function
GO:0005102 signaling receptor binding
GO:0030674 protein-macromolecule adaptor activity
GO:0046872 metal ion binding
Biological Process
GO:0007160 cell-matrix adhesion
GO:0007596 blood coagulation
GO:0030168 platelet activation
GO:0051258 protein polymerization
GO:0070527 platelet aggregation
GO:0072378 blood coagulation, fibrin clot formation
Cellular Component
GO:0005576 extracellular region
GO:0005577 fibrinogen complex
GO:0005615 extracellular space
GO:0062023 collagen-containing extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1m1j, PDBe:1m1j, PDBj:1m1j
PDBsum1m1j
PubMed11601975
UniProtQ02020|FIBB_CHICK Fibrinogen beta chain (Fragment) (Gene Name=FGB)

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