Structure of PDB 1e03 Chain L

Receptor sequence
>1e03L (length=423) Species: 9606 (Homo sapiens) [Search protein sequence]
VDICTAKPRDIPMNPMCIYRSPEEDEGSEQKIPEATNRRVWELSKANSRF
ATTFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKF
DTISEKTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETY
QDISELVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAIN
ELTVLVLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKF
RYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWL
DELEEMMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEG
RDDLYVSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLNPNRVTFKANRPF
LVFIREVPLNTIIFMGRVANPCV
3D structure
PDB1e03 Structure of Beta-Antithrombin and the Effect of Glycosylation on Antithrombin'S Heparin Affinity and Activity.
ChainL
Resolution2.9 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 Z9L L R13 R47 K114 R9 R39 K106
BS02 Z9K L R47 K114 R39 K106
BS03 GU6 L P12 R13 K114 F122 P8 R9 K106 F114
BS04 GU1 L K11 N45 K7 N37
BS05 Z9H L A43 T44 N45 R129 A35 T36 N37 R121
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:1e03, PDBe:1e03, PDBj:1e03
PDBsum1e03
PubMed12581643
UniProtP01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)

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