Structure of PDB 1r1l Chain I Binding Site BS01

Receptor Information
>1r1l Chain I (length=416) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDICTAKPRDIPMNPMCIYRSPEKKPEATNRRVWELSKANSRFATTFYQH
LADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKT
SDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELV
YGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVL
VNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAE
GTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMM
LVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVS
DAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREV
PLNTIIFMGRVANPCV
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1r1l Serpins and the design of peptides to block intermolecular beta-linkages
Resolution2.7 Å
Binding residue
(original residue number in PDB)		V190 R197 I198 N217 T218 I219 Y220 F221 K222 G223 W225 F274 H369 K370 A371 F372 L373 E374 V375 N376 F422
Binding residue
(residue number reindexed from 1)		V175 R182 I183 N202 T203 I204 Y205 F206 K207 G208 W210 F259 H354 K355 A356 F357 L358 E359 V360 N361 F407
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
PDBsum1r1l
PubMed
UniProtP01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)

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