General information
PDB ID 1HAP
Title COMPLEX OF HUMAN ALPHA-THROMBIN WITH A 15MER OLIGONUCLEOTIDE GGTTGGTGTGGTTGG (BASED ON X-RAY MODEL OF DNA)
PDB header HYDROLASE/HYDROLASE INHIBITOR/DNA
Date 1995-10-03
Experimental method X-RAY DIFFRACTION
Resolution (A) 2.8
Kind dna
Organism HOMO SAPIENS
Download
complex
View in
Jmol
Quick Links
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:
pdb1hap.pdb LH D 0
Biounits:
1hap.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 2.6e-15 1 No_clan L 1 14
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 extracellular space
H=364-622, L=328-363 C endoplasmic reticulum lumen
H=364-622, L=328-363 C Golgi lumen
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 thrombospondin receptor activity
H=364-622, L=328-363 F calcium ion binding
H=364-622, L=328-363 P positive regulation of phosphatidylinositol 3-kinase cascade
H=364-622, L=328-363 P platelet activation
H=364-622, L=328-363 P positive regulation of reactive oxygen species metabolic process
H=364-622, L=328-363 P proteolysis
H=364-622, L=328-363 P positive regulation of release of sequestered calcium ion into cytosol
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 fibrinolysis
H=364-622, L=328-363 P negative regulation of fibrinolysis
H=364-622, L=328-363 P positive regulation of protein phosphorylation
H=364-622, L=328-363 P cell surface receptor signaling pathway
H=364-622, L=328-363 P peptidyl-glutamic acid carboxylation
H=364-622, L=328-363 P cytosolic calcium ion homeostasis
H=364-622, L=328-363 P leukocyte migration
H=364-622, L=328-363 P positive regulation of collagen biosynthetic process
H=364-622, L=328-363 P negative regulation of astrocyte differentiation
H=364-622, L=328-363 P positive regulation of cell growth
H=364-622, L=328-363 P negative regulation of proteolysis
H=364-622, L=328-363 P negative regulation of platelet activation
H=364-622, L=328-363 P post-translational protein modification
H=364-622, L=328-363 P regulation of cell shape
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 positive regulation of cell proliferation
Sequences
Download file with secondary structure created by Stride  
1hap.pdb1.pdb:   [ download sequences in FASTA format ]
D (dna): 
Click "SHOW" for view sequence
H (protein): 
Click "SHOW" for view sequence
L (protein): 
Click "SHOW" for view sequence
© NPIDB team 2003 - 2020

text