Structure of PDB 6bjr Chain A

Receptor sequence
>6bjrA (length=575) Species: 9606 (Homo sapiens) [Search protein sequence]
ANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETA
RTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEIN
CTTHPGADLQENFCRNPDSSTMGPWCYTTDPTVRRQECSIPVCGQDQVTV
AMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAK
ALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEE
AVEEETGDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDK
TERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRW
VLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIH
PRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGR
VTGWGNLKETWTCNVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFC
AGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGEYLE
3D structure
PDB6bjr Structure of prothrombin in the closed form reveals new details on the mechanism of activation.
ChainA
Resolution6.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H363 D419 E522 G523 D524 S525
Catalytic site (residue number reindexed from 1) H356 D412 E515 G516 D517 S518
Enzyme Commision number 3.4.21.5: thrombin.
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 MG A A30 E32 A30 E32
BS02 MG A E25 E29 E25 E29
BS03 MG A E25 E26 E29 E25 E26 E29
BS04 MG A E26 E29 E26 E29
BS05 MG A E16 E26 E16 E26
BS06 MG A E14 E19 R54 E14 E19 R54
Gene Ontology
Molecular Function
GO:0001530 lipopolysaccharide binding
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005102 signaling receptor binding
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008083 growth factor activity
GO:0008201 heparin binding
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0048018 receptor ligand activity
GO:0070053 thrombospondin receptor activity
Biological Process
GO:0001934 positive regulation of protein phosphorylation
GO:0006508 proteolysis
GO:0006953 acute-phase response
GO:0007166 cell surface receptor signaling pathway
GO:0007186 G protein-coupled receptor signaling pathway
GO:0007596 blood coagulation
GO:0008284 positive regulation of cell population proliferation
GO:0008360 regulation of cell shape
GO:0009611 response to wounding
GO:0010468 regulation of gene expression
GO:0010544 negative regulation of platelet activation
GO:0030168 platelet activation
GO:0030193 regulation of blood coagulation
GO:0030194 positive regulation of blood coagulation
GO:0030195 negative regulation of blood coagulation
GO:0030307 positive regulation of cell growth
GO:0032024 positive regulation of insulin secretion
GO:0032967 positive regulation of collagen biosynthetic process
GO:0042730 fibrinolysis
GO:0045861 negative regulation of proteolysis
GO:0046427 positive regulation of receptor signaling pathway via JAK-STAT
GO:0048712 negative regulation of astrocyte differentiation
GO:0051281 positive regulation of release of sequestered calcium ion into cytosol
GO:0051480 regulation of cytosolic calcium ion concentration
GO:0051838 cytolysis by host of symbiont cells
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
GO:0051918 negative regulation of fibrinolysis
GO:0061844 antimicrobial humoral immune response mediated by antimicrobial peptide
GO:0070945 neutrophil-mediated killing of gram-negative bacterium
GO:0090218 positive regulation of lipid kinase activity
GO:1900016 negative regulation of cytokine production involved in inflammatory response
GO:1900182 positive regulation of protein localization to nucleus
GO:1900738 positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
GO:1990806 ligand-gated ion channel signaling pathway
GO:2000379 positive regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005788 endoplasmic reticulum lumen
GO:0005796 Golgi lumen
GO:0005886 plasma membrane
GO:0009897 external side of 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:6bjr, PDBe:6bjr, PDBj:6bjr
PDBsum6bjr
PubMed29440720
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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