PDBsum entry 2gch

Hydrolase (serine proteinase)

PDB id: 2gch

Contents

Protein chains

11 a.a.

131 a.a.

95 a.a.

Waters ×151

References listed in PDB file

Key reference

Title

Refined crystal structure of gamma-Chymotrypsin at 1.9 a resolution. Comparison with other pancreatic serine proteases.

Authors

G.H.Cohen, E.W.Silverton, D.R.Davies.

Ref.

J Mol Biol, 1981, 148, 449-479. [DOI no: 10.1016/0022-2836(81)90186-8]

PubMed id

6914398

Abstract

No abstract given.

Figure 1.
IG. . The progress of the partial refinement f tosyl-y-CHT nd, subsequently, native yCHT is shown. he left-hand curve refers to the osyl-y-CHT (2.7 ) and the right-hand one to the naive y-HT (1.9A). The refinement method is indicated along the horizontal bar in the igure sing the code: RS(m.i.r.). real-space mehod on .i.r. aps; S(ZF,-FJ. real-space method n 2F- F, aps; DDF, differential difference Fourier; Lt51, least-squares series 1; S2, least-squares series 2. The -factor is defined in the onventional manner as H = [[F,,[ - IF,II/x IF,], ere F, s an observed structure factor and F, is calculated tructure factor.

Figure 4.
FIG. 4. ntermolewlar nteractions in y-(`HI' bout the q-stallographic 4, axis n he vicinity fthr ac*tive cente. Residues of the nteracting molewles are distinguished bv using open and losed ckles. There are no lose ntermolecular contacts formed with he active-center residue. The ollowing intermolecular int,eractions denoted g thin ines) an e seen: ys90 N-sp64 61, ys90 N-(;11y59 0 and Phe41 0-Seti Oy. In addition, ater molecules 440 nd 54 form ridges between the 2 olecules.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1981, 148, 449-479) copyright 1981.

Secondary reference #1

Title

The stereochemistry of substrate binding to chymotrypsin a .

Authors

D.M.Segal, C.H.Cohen, D.R.Davies, J.C.Powers, P.E.Wilcox.

Ref.

Cold Spring Harb Symp Quant Biol, 1972, 36, 85-90.

PubMed id

4508176

Secondary reference #2

Title

Substrate binding site in bovine chymotrypsin a-Gamma. A crystallographic study using peptide chloromethyl ketones as site-Specific inhibitors.

Authors

D.M.Segal, J.C.Powers, G.H.Cohen, D.R.Davies, P.E.Wilcox.

Ref.

Biochemistry, 1971, 10, 3728-3738. [DOI no: 10.1021/bi00796a014]

PubMed id

5107010

Secondary reference #3

Title

The relation between gamma-And alpha-Chymotrypsin. Ii. Direct comparison of the electron densities at 5-5 angstrom resolution.

Authors

G.H.Cohen, B.W.Matthews, D.R.Davies.

Ref.

Acta Crystallogr B, 1970, 26, 1062-1069.

PubMed id

5537151

Secondary reference #4

Title

Structure of gamma-Chymotrypsin at 5.5 a resolution.

Authors

G.H.Cohen, E.W.Silverton, B.W.Matthews, H.Braxton, D.R.Davies.

Ref.

J Mol Biol, 1969, 44, 129-141. [DOI no: 10.1016/0022-2836(69)90409-4]

PubMed id

5822897

Figure 1.
FIG. 1. Projected difference Fourier eynthesis of PMMMBS- verBus osyl-yCHT. Phaacs are based on pipsyl- vereua tosyl-yCHT. The two peaks correspond to two mecury atoms in equivalent positions related by a 2-fold axis.

Figure 2.
FIG. 2. Projected difference Fourier synthesis of iodineted yCHT mius native yCHT. Phases are based on pipsyl- z)erBuB tosyl-yCHT. The six peaks correspond to iodine atoms in three binding sites, one strong and two weak.

The above figures are reproduced from the cited reference with permission from Elsevier

Secondary reference #5

Title

Relation between gamma- And alpha-Chymotrypsin.

Authors

B.W.Matthews, G.H.Cohen, E.W.Silverton, H.Braxton, D.R.Davies.

Ref.

J Mol Biol, 1968, 36, 179-183.

PubMed id

5760536

Secondary reference #6

Title

An isomorphous heavy atom substitution at the active site of gamma-Chymotrypsin.

Authors

P.B.Sigler, H.C.Skinner, C.L.Coulter, J.Kallos, H.Braxton, D.R.Davies.

Ref.

Proc Natl Acad Sci U S A, 1964, 51, 1146-1151.

PubMed id

14215636