Structure of PDB 1r1l Chain I Binding Site BS02
Receptor Information
>1r1l Chain I (length=416) Species:
9606
(Homo sapiens) [
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VDICTAKPRDIPMNPMCIYRSPEKKPEATNRRVWELSKANSRFATTFYQH
LADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKT
SDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELV
YGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVL
VNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE
GTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMM
LVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVS
DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREV
PLNTIIFMGRVANPCV
Ligand information
>1r1l Chain D (length=3) [
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LLF
Receptor-Ligand Complex Structure
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PDB
1r1l
Serpins and the design of peptides to block intermolecular beta-linkages
Resolution
2.7 Å
Binding residue
(original residue number in PDB)
F87 T90 V212 L213 V214 L215 Y363 V364 S365 D366
Binding residue
(residue number reindexed from 1)
F72 T75 V197 L198 V199 L200 Y348 V349 S350 D351
Enzymatic activity
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0002020
protease binding
GO:0004867
serine-type endopeptidase inhibitor activity
GO:0005515
protein binding
GO:0008201
heparin binding
GO:0042802
identical protein binding
Biological Process
GO:0007596
blood coagulation
GO:0010466
negative regulation of peptidase activity
GO:0030193
regulation of blood coagulation
Cellular Component
GO:0005576
extracellular region
GO:0005615
extracellular space
GO:0005788
endoplasmic reticulum lumen
GO:0005886
plasma membrane
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:1r1l
,
PDBe:1r1l
,
PDBj:1r1l
PDBsum
1r1l
PubMed
UniProt
P01008
|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)
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