spacer
spacer
Go to PDB code: 
protein Protein-protein interface(s) links
Proteinase inhibitor (kazal) PDB-id
1ovo
Biological unit* = asymmetric unit, as shown
(*as deduced by PQS)
Main view
    Jmol     Help!  
Contents
Description
Header details
Header records
References
PROCHECK
Protein chains
56 a.a. *
Waters ×46

* Residue conservation analysis
Tools
Image Generation
AstexViewer™@PDBe
Run PROCHECK
Clefts Calculation
  
Right view Bottom view
PDB id: 1ovo
Name: Proteinase inhibitor (kazal)
Title: Crystallographic refinement of japanese quail ovomucoid, a kazal-type inhibitor, and model building studies of complexes with serine proteases

Structure:
Ovomucoid third domain. Chain: a, b, c, d. Engineered: yes

Source:
Coturnix japonica. Japanese quail. Organism_taxid: 93934

Biological unit:
Tetramer (from PQS)

UniProt:
Chains A, B, C, D: P01003 (IOVO_COTJA)
Pfam   ArchSchema ?
Seq: 186 a.a.
Struc: 56 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
1.90Å

R-factor:
not given

Authors:
E.Weber,E.Papamokos,W.Bode,R.Huber,I.Kato,M.Laskowskijunior

Key ref:
E.Papamokos et al. (1982). Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.. J Mol Biol, 158, 515-537. [PubMed id: 6752426] [DOI: 10.1016/0022-2836(82)90212-1]

Date:
18-Jan-82

Release date:
26-May-82
Quick_links
RCSB
PDBe
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
ProSAT
Whatcheck
Procheck
Go to PROCHECK summary
Surface
RasMol surface
spacer
spacer

 
    Key reference    
 
 
DOI no: 10.1016/0022-2836(82)90212-1 J Mol Biol 158:515-537 (1982)
PubMed id: 6752426  
 
 
Crystallographic refinement of Japanese quail ovomucoid, a Kazal-type inhibitor, and model building studies of complexes with serine proteases.
E.Papamokos, E.Weber, W.Bode, R.Huber, M.W.Empie, I.Kato, M.Laskowski.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 2.
IG:. 2. St,rreo drawing of the C'' and side -chain arrangement of OMJl'Q3 (m&rule 1)
Figure 5.
FIG:. 5. )istril)ution of B-values of molecnlrs 1 ( x ) and 1 (0) (a). The B-values of t,he main-chains wew plotted after avraging the individual VHIIIVS of C'``. Co. S. (`. 0 for each residur. (t)) Thr sarw for molrcllles 3 ( x ) nd 4 (0).
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1982, 158, 515-537) copyright 1982.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
15162493 A.Berchanski, B.Shapira, and M.Eisenstein (2004).
Hydrophobic complementarity in protein-protein docking.
  Proteins, 56, 130-142.  
11847280 A.Heifetz, E.Katchalski-Katzir, and M.Eisenstein (2002).
Electrostatics in protein-protein docking.
  Protein Sci, 11, 571-587.  
12186551 H.Hemmi, T.Yoshida, T.Kumazaki, N.Nemoto, J.Hasegawa, F.Nishioka, Y.Kyogoku, H.Yokosawa, and Y.Kobayashi (2002).
Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy.
  Biochemistry, 41, 10657-10664.
PDB code: 1iw4
11685246 S.Ye, A.L.Cech, R.Belmares, R.C.Bergstrom, Y.Tong, D.R.Corey, M.R.Kanost, and E.J.Goldsmith (2001).
The structure of a Michaelis serpin-protease complex.
  Nat Struct Biol, 8, 979-983.
PDB codes: 1i99 1k9o
10891089 W.R.Forsyth, and A.D.Robertson (2000).
Insensitivity of perturbed carboxyl pK(a) values in the ovomucoid third domain to charge replacement at a neighboring residue.
  Biochemistry, 39, 8067-8072.  
10081963 J.A.Cuff, and G.J.Barton (1999).
Evaluation and improvement of multiple sequence methods for protein secondary structure prediction.
  Proteins, 34, 508-519.  
  9514268 J.Liu, Y.Gong, O.Prakash, L.Wen, I.Lee, J.K.Huang, and R.Krishnamoorthi (1998).
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
  Protein Sci, 7, 132-141.  
9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
  Annu Rev Biophys Biomol Struct, 26, 597-627.  
  8535235 K.Huang, W.Lu, S.Anderson, M.Laskowski, and M.N.James (1995).
Water molecules participate in proteinase-inhibitor interactions: crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B.
  Protein Sci, 4, 1985-1997.
PDB codes: 1sgp 1sgq 1sgr
  7703840 D.V.Laurents, S.Subbiah, and M.Levitt (1994).
Different protein sequences can give rise to highly similar folds through different stabilizing interactions.
  Protein Sci, 3, 1938-1944.  
  7920265 S.Bromberg, and K.A.Dill (1994).
Side-chain entropy and packing in proteins.
  Protein Sci, 3, 997.  
8456095 G.Müller, M.Gurrath, M.Kurz, and H.Kessler (1993).
Beta VI turns in peptides and proteins: a model peptide mimicry.
  Proteins, 15, 235-251.  
8427637 P.C.Sil, T.K.Chaudhuri, and N.K.Sinha (1993).
Basic trypsin-subtilisin inhibitor from marine turtle egg white: hydrodynamic and inhibitory properties.
  J Protein Chem, 12, 71-78.  
1541261 W.Bode, and R.Huber (1992).
Natural protein proteinase inhibitors and their interaction with proteinases.
  Eur J Biochem, 204, 433-451.  
  1772402 S.D.Patterson, K.Bell, and D.C.Shaw (1991).
The equine major plasma serpin multigene family: partial characterization including sequence of the reactive-site regions.
  Biochem Genet, 29, 477-499.  
2278733 M.Bolognesi, L.Pugliese, G.Gatti, F.Frigerio, A.Coda, L.Antolini, H.P.Schnebli, E.Menegatti, G.Amiconi, and P.Ascenzi (1990).
X-ray crystal structure of the bovine alpha-chymotrypsin/eglin c complex at 2.6 A resolution.
  J Mol Recognit, 3, 163-168.  
2577843 R.Wang, R.J.Cotter, T.Y.Lin, and M.Laskowski (1988).
Plasma desorption mass spectrometric analysis of glycosylated ovomucoid third domain from Japanese quail.
  Rapid Commun Mass Spectrom, 2, 71-73.  
3663857 L.G.Presta, and E.F.Meyer (1987).
Prediction of protein--ligand interactions: the complex of porcine pancreatic elastase with a valine-derived benzoxazinone.
  Biopolymers, 26, 1207-1225.  
3301348 W.Bode, E.Papamokos, and D.Musil (1987).
The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.
  Eur J Biochem, 166, 673-692.
PDB code: 1cse
3310077 W.Braun (1987).
Distance geometry and related methods for protein structure determination from NMR data.
  Q Rev Biophys, 19, 115-157.  
3814765 J.J.Beintema (1986).
Do asparagine-linked carbohydrate chains in glycoproteins have a preference for beta-bends?
  Biosci Rep, 6, 709-714.  
3711152 J.L.Markley, D.H.Croll, R.Krishnamoorthi, G.Ortiz-Polo, W.M.Westler, W.C.Bogard, and M.Laskowski (1986).
One- and two-dimensional NMR spectral analysis of the consequences of single amino acid replacements in proteins.
  J Cell Biochem, 30, 291-309.  
  3640709 W.Bode, A.Z.Wei, R.Huber, E.Meyer, J.Travis, and S.Neumann (1986).
X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor.
  EMBO J, 5, 2453-2458.
PDB code: 1ppf
  3519213 W.Bode, E.Papamokos, D.Musil, U.Seemueller, and H.Fritz (1986).
Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.
  EMBO J, 5, 813-818.  
16593622 C.A.McPhalen, I.Svendsen, I.Jonassen, and M.N.James (1985).
Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin Novo.
  Proc Natl Acad Sci U S A, 82, 7242-7246.  
3971987 W.Bode, O.Epp, R.Huber, M.Laskowski, and W.Ardelt (1985).
The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3).
  Eur J Biochem, 147, 387-395.
PDB code: 2ovo
6673759 R.Huber, and W.S.Bennett (1983).
Functional significance of flexibility in proteins.
  Biopolymers, 22, 261-279.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.