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PDBsum entry 4dih

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protein dna_rna ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor/DNA PDB id
4dih

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
27 a.a.
249 a.a.
DNA/RNA
Ligands
0G6
NAG
_NA ×2
Metals
_ZN ×3
_CL ×2
Waters ×217
PDB id:
4dih
Name: Hydrolase/hydrolase inhibitor/DNA
Title: X-ray structure of the complex between human alpha thrombin and thrombin binding aptamer in the presence of sodium ions
Structure: Prothrombin. Chain: l. Fragment: light chain fragment (unp residues 328-363). Synonym: coagulation factor ii, thrombin light chain. Prothrombin. Chain: h. Fragment: heavy chain fragment (unp residues 364-622). Synonym: coagulation factor ii, thrombin heavy chain. Thrombin binding aptamer.
Source: Homo sapiens. Human. Organism_taxid: 9606. Synthetic: yes. Synthetic DNA. Organism_taxid: 32630
Resolution:
1.80Å     R-factor:   0.167     R-free:   0.213
Authors: I.Russo Krauss,A.Merlino,L.Mazzarella,F.Sica
Key ref: I.Russo Krauss et al. (2012). High-resolution structures of two complexes between thrombin and thrombin-binding aptamer shed light on the role of cations in the aptamer inhibitory activity. Nucleic Acids Res, 40, 8119-8128. PubMed id: 22669903
Date:
31-Jan-12     Release date:   18-Jul-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00734  (THRB_HUMAN) -  Prothrombin from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
622 a.a.
27 a.a.
Protein chain
Pfam   ArchSchema ?
P00734  (THRB_HUMAN) -  Prothrombin from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
622 a.a.
249 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chain
  G-G-T-T-G-G-T-G-T-G-G-T-T-G-G 15 bases

 Enzyme reactions 
   Enzyme class: Chains L, H: E.C.3.4.21.5  - thrombin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Arg-|-Gly; activates fibrinogen to fibrin and releases fibrinopeptide A and B.

 

 
Nucleic Acids Res 40:8119-8128 (2012)
PubMed id: 22669903  
 
 
High-resolution structures of two complexes between thrombin and thrombin-binding aptamer shed light on the role of cations in the aptamer inhibitory activity.
I.Russo Krauss, A.Merlino, A.Randazzo, E.Novellino, L.Mazzarella, F.Sica.
 
  ABSTRACT  
 
No abstract given.

 

 

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