General information
PDB ID 1HUT
Title THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER
PDB header HYDROLASE/HYDROLASE INHIBITOR/DNA
Date 1993-05-27
Experimental method X-RAY DIFFRACTION
Resolution (A) 2.9
Kind dna
Organism HOMO SAPIENS
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PDB PDBe MMDB Jena OCA
CATH PDBsum HSSP PDBePISA UniProt
ProteopediA BIPA
Composition of PDB entry and biounits
File: Protein chains: DNA chains: RNA chains: No. of models: Action:
PDB entry:
pdb1hut.pdb LH D 0
Biounits:
1hut.pdb1.pdb LH D 1
Pfam domains
Name: Type: Domain: E-value: Significance: Clan: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
Trypsin Domain P00734_364-613 4.4e-70 1 CL0124 H 16 238 D   
Thrombin_light Domain P00734_328-363 5.4e-22 1 No_clan L 1 15   
SCOP domains
Classification: Protein: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
Class: All beta proteins
  Fold: Trypsin-like serine proteases
    Superfamily: Trypsin-like serine proteases
      Family: Eukaryotic proteases
Thrombin H N/A N/A D -
Class: All beta proteins
  Fold: Trypsin-like serine proteases
    Superfamily: Trypsin-like serine proteases
      Family: Eukaryotic proteases
Thrombin L N/A N/A D -
Class: All beta proteins
  Fold: Trypsin-like serine proteases
    Superfamily: Trypsin-like serine proteases
      Family: Eukaryotic proteases
Thrombin H N/A N/A -
Class: All beta proteins
  Fold: Trypsin-like serine proteases
    Superfamily: Trypsin-like serine proteases
      Family: Eukaryotic proteases
Thrombin L N/A N/A -
GO terms
Protein chains: GO type: GO description:
H=364-622, L=328-363 C Golgi lumen
H=364-622, L=328-363 C endoplasmic reticulum lumen
H=364-622, L=328-363 C extracellular space
H=364-622, L=328-363 C plasma membrane
H=364-622, L=328-363 F serine-type endopeptidase activity
H=364-622, L=328-363 F calcium ion binding
H=364-622, L=328-363 F thrombospondin receptor activity
H=364-622, L=328-363 P proteolysis
H=364-622, L=328-363 P cytosolic calcium ion homeostasis
H=364-622, L=328-363 P positive regulation of cell growth
H=364-622, L=328-363 P positive regulation of protein phosphorylation
H=364-622, L=328-363 P negative regulation of proteolysis
H=364-622, L=328-363 P positive regulation of phosphatidylinositol 3-kinase cascade
H=364-622, L=328-363 P blood coagulation, intrinsic pathway
H=364-622, L=328-363 P acute-phase response
H=364-622, L=328-363 P regulation of cell shape
H=364-622, L=328-363 P cell surface receptor signaling pathway
H=364-622, L=328-363 P positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway
H=364-622, L=328-363 P positive regulation of collagen biosynthetic process
H=364-622, L=328-363 P leukocyte migration
H=364-622, L=328-363 P negative regulation of platelet activation
H=364-622, L=328-363 P fibrinolysis
H=364-622, L=328-363 P positive regulation of reactive oxygen species metabolic process
H=364-622, L=328-363 P peptidyl-glutamic acid carboxylation
H=364-622, L=328-363 P negative regulation of fibrinolysis
H=364-622, L=328-363 P post-translational protein modification
H=364-622, L=328-363 P positive regulation of cell proliferation
H=364-622, L=328-363 P positive regulation of release of sequestered calcium ion into cytosol
H=364-622, L=328-363 P platelet activation
H=364-622, L=328-363 P negative regulation of astrocyte differentiation
Sequences
Download file with secondary structure created by Stride  
1hut.pdb1.pdb:   [ download sequences in FASTA format ]
D (dna): 
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H (protein): 
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L (protein): 
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