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PDBsum entry 2ptc

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Complex (proteinase/inhibitor) PDB id
2ptc
Contents
Protein chains
223 a.a. *
58 a.a. *
Metals
_CA
Waters ×157
* Residue conservation analysis

References listed in PDB file
Key reference
Title The geometry of the reactive site and of the peptide groups in trypsin, Trypsinogen and its complexes with inhibitors
Authors M.Marquart, J.Walter, J.Deisenhofer, W.Bode, R.Huber.
Ref. Acta Crystallogr ,Sect B, 1983, 39, 480.
Secondary reference #1
Title Structural studies on the pancreatic trypsin inhibitor-Trypsin complex and its free components. Structure and function relationships in serine protease inhibition and catalysis
Authors W.Bode, P.Schwager, R.Huber.
Ref. Miami Winter Symp, 1976, 11, 43.
Secondary reference #2
Title The structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor III. Structure of the anhydro-Trypsin-Inhibitor complex.
Authors R.Huber, W.Bode, D.Kukla, U.Kohl, C.A.Ryan.
Ref. Biophys Struct Mech, 1975, 1, 189-201.
PubMed id 1086102
Abstract
Secondary reference #3
Title The single calcium-Binding site of crystallin bovin beta-Trypsin.
Authors W.Bode, P.Schwager.
Ref. FEBS Lett, 1975, 56, 139-143. [DOI no: 10.1016/0014-5793(75)80128-1]
PubMed id 1157929
Full text Abstract
Secondary reference #4
Title Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Refinement of the crystal structure analysis
Authors R.Huber, D.Kukla, W.Steigemann, J.Deisenhofer, A.Jones.
Ref. Bayer Symp, 1974, 5, 497.
Secondary reference #5
Title Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Ii. Crystallographic refinement at 1.9 a resolution.
Authors R.Huber, D.Kukla, W.Bode, P.Schwager, K.Bartels, J.Deisenhofer, W.Steigemann.
Ref. J Mol Biol, 1974, 89, 73. [DOI no: 10.1016/0022-2836(74)90163-6]
PubMed id 4475115
Full text Abstract
Figure 2.
FIG. 2. Final difference Fourier mp at Tyr 69. Contours from O-1 e/A3 in 0.06 e/A3 steps. Solid lines indicate positive, broken lines negative residual density. The aromaic ring is mobile rotating around 2'.
Figure 7.
FI. 7. Lys 15 (I) amide. The Lys 15 (I) 0 is -34'' out of the plane formed by 0, C, N. It is strongly deformed towards a tetrahedral carbon. Ala 16 (I) Cfl is in the upper right-hand corner.
The above figures are reproduced from the cited reference with permission from Elsevier
Secondary reference #6
Title Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region.
Authors A.Rühlmann, D.Kukla, P.Schwager, K.Bartels, R.Huber.
Ref. J Mol Biol, 1973, 77, 417-436. [DOI no: 10.1016/0022-2836(73)90448-8]
PubMed id 4737866
Full text Abstract
Figure 2.
FIG. . For legend see Fig. 2.
Figure 5.
IG. 5. For legend see Fig. 2,
The above figures are reproduced from the cited reference with permission from Elsevier
PROCHECK
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