Structure of PDB 1tb6 Chain I

Receptor sequence
>1tb6I (length=412) Species: 9606 (Homo sapiens) [Search protein sequence]
PVDICTAKPRDIPMNPMCIYRSPEQKIPEATNRRVWELSKANSRFATTFY
QHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISE
KTSDQIHFFFAKLNCRLYRKANKASKLVSANRLFGDKSLTFNETYQDISE
LVYGAKLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVL
VLVNTIYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRV
AEGTQVLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEE
MMLCVHMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLY
VSDAFHKAFLEVNEEGTAVVIAGRSLNPNRVCFKANRPFLVFIREVPLNT
IIFMGRVANPCV
3D structure
PDB1tb6 Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.
ChainI
Resolution2.5 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 GU3 I R47 S112 E113 K114 R34 S99 E100 K101
BS02 GU2 I R46 R47 K114 R33 R34 K101
BS03 GU6 I P12 R13 N45 K114 P9 R10 N32 K101
BS04 GU1 I K11 R46 K125 K8 R33 K112
BS05 GU5 I T44 N45 R129 T31 N32 R116
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:1tb6, PDBe:1tb6, PDBj:1tb6
PDBsum1tb6
PubMed15311269
UniProtP01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)

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