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Contents |
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34 a.a.*
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257 a.a.*
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65 a.a.*
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* Residue conservation analysis
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* C-alpha coords only
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PDB id:
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Hydrolase(serine protease)
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Title:
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The structure of a complex of recombinant hirudin and human alpha- thrombin
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Structure:
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Alpha-thrombin (small subunit). Chain: l. Engineered: yes. Alpha-thrombin (large subunit). Chain: h. Engineered: yes. Hirudin variant 2. Chain: i. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Hirudinaria manillensis. Organism_taxid: 6419
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Biol. unit:
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Not given
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Resolution:
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Authors:
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A.Tulinsky,T.J.Rydel,K.G.Ravichandran,R.Huber,W.Bode
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Key ref:
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T.J.Rydel
et al.
(1990).
The structure of a complex of recombinant hirudin and human alpha-thrombin.
Science,
249,
277-280.
PubMed id:
DOI:
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Date:
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11-Jun-93
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Release date:
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31-Jan-94
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Headers
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References
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P00734
(THRB_HUMAN) -
Prothrombin from Homo sapiens
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Seq:
Struc:
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622 a.a.
34 a.a.
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Enzyme class:
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Chains L, H:
E.C.3.4.21.5
- thrombin.
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Reaction:
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Preferential cleavage: Arg-|-Gly; activates fibrinogen to fibrin and releases fibrinopeptide A and B.
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DOI no:
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Science
249:277-280
(1990)
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PubMed id:
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The structure of a complex of recombinant hirudin and human alpha-thrombin.
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T.J.Rydel,
K.G.Ravichandran,
A.Tulinsky,
W.Bode,
R.Huber,
C.Roitsch,
J.W.Fenton.
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ABSTRACT
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The crystallographic structure of a recombinant hirudin-thrombin complex has
been solved at 2.3 angstrom (A) resolution. Hirudin consists of an NH2-terminal
globular domain and a long (39 A) COOH-terminal extended domain. Residues Ile1
to Tyr3 of hirudin form a parallel beta-strand with Ser214 to Glu217 of thrombin
with the nitrogen atom of Ile1 making a hydrogen bond with Ser195 O gamma atom
of the catalytic site, but the specificity pocket of thrombin is not involved in
the interaction. The COOH-terminal segment makes numerous electrostatic
interactions with an anion-binding exosite of thrombin, whereas the last five
residues are in a helical loop that forms many hydrophobic contacts. In all, 27
of the 65 residues of hirudin have contacts less than 4.0 A with thrombin (10
ion pairs and 23 hydrogen bonds). Such abundant interactions may account for the
high affinity and specificity of hirudin.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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PDB codes:
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|
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and
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PDB code:
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and
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|
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PDB code:
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PDB code:
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Biopolymers,
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|
| |
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PDB code:
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| |
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PDB code:
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PDB code:
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| |
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|
PDB codes:
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|
|
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|
|
|
I.M.Francischetti,
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| |
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| |
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|
PDB code:
|
|
|
|
|
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|
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| |
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PDB code:
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Where a reference describes a PDB structure, the PDB
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