Structure of PDB 1m1j Chain E Binding Site BS01
Receptor Information
>1m1j Chain E (length=401) Species:
9031
(Gallus gallus) [
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IYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKF
SDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNL
DNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVS
GRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQD
GSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPT
KVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGAS
QLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCH
AANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYF
P
Ligand information
>1m1j Chain J (length=4) [
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GHRP
Receptor-Ligand Complex Structure
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PDB
1m1j
Crystal Structure of Native Chicken Fibrinogen at 2.7 A Resolution
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
L364 M371 W389 E401 D402 R410 C411 H412 T435 D436 M442
Binding residue
(residue number reindexed from 1)
L302 M309 W327 E339 D340 R348 C349 H350 T373 D374 M380
Enzymatic activity
Enzyme Commision number
?
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
PDBsum
1m1j
PubMed
11601975
UniProt
Q02020
|FIBB_CHICK Fibrinogen beta chain (Fragment) (Gene Name=FGB)
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