Structure of PDB 3evj Chain L

Receptor sequence
>3evjL (length=417) Species: 9606 (Homo sapiens) [Search protein sequence]
VDICTAKPRDIPMNPMCIYREGSEQKIPEATNRRVWELSKANSRFATTFY
QHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISE
KTSDQIHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISE
LVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVL
VLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRV
AEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEE
MMLVVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLY
VSDAFHKAFLEVNEEGSEAAASTAVVIAGRSLPNRVTFKANRPFLVFIRE
VPLNTIIFMGRVANPCV
3D structure
PDB3evj The critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin.
ChainL
Resolution3.0 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 ZDO L R47 S112 K114 R34 S99 K101
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:3evj, PDBe:3evj, PDBj:3evj
PDBsum3evj
PubMed19452598
UniProtP01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)

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