(BOVINE TRYPSIN)Authors: Brzuszkiewicz,A. ,Dauter, M., Dauter, Z.
Picture of Bovine Trypsin in 3DBismillahirahmanirrahim. Alhamdulillah, today I want to introduce to all of you about the structure of BOVINE TRYPSIN in 3D and the structure of ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,D-ACD2AB (UNEXPOSED). Thank you so much to my computer in science lecturer Madam Linda for teaching me this subject for this semester. This topic is quite interesting.I like it so much.
We can see the real of any protein structure in 3D that we can observe it clearly on any parts of proteins structure that we like via using RASWIN software.
Molecular Description : Polymer : 1
Scientific Name :
Bos taurus Common Name : Bovine
Classification : Hydrolase
Structure Weight: 23672.79
Molecule:Cationic trypsin
Polymer : 1 Type: polypeptide(L) Length: 223
Chains : A
EC# : 3.4.21.4 Go to IUBMB EC entry
Fragment: residues 24-246
Classification: Hydrolase
Experiment: X-RAY DIFFRACTION with resolution of 0.80 Å
Compound: 1 Polymer [ Display Full Polymer Details | Display for All Results ]
Molecule: Cationic trypsin
Polymer : 1 Type: polypeptide(L) Length: 223
Chains : A
EC# : 3.4.21.4
Fragment: residues 24-246
4 Ligands
Identifier Name FormulaBEN BENZAMIDINE C7 H8 N2
CA CALCIUM ION Ca
GOL GLYCEROL C3 H8 O3
SO4 SULFATE ION O4 S
Citation: Not Available.
Molecule of the Month: Thrombin, Trypsin, Serpins, Tissue Factor, Fibrin
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ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,D-ACD2AB (UNEXPOSED) Authors:
Ge, W., Clifton, I.J., Adlington, R.M., Baldwin, J.E., Rutledge, P.J.
Scientific Name : Emericella nidulans
Expression System: Escherichia coli
This is the picture of ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,D-ACD2AB Classification: Oxidoreductase
Experiment : X-RAY DIFFRACTION with resolution of 2.50 Å
Compound : 1 Polymer
Molecule : ISOPENICILLIN N SYNTHASE
Polymer : 1 Type: polypeptide(L) Length: 331
Chains : A
EC# : 1.21.3.1
2 Ligands
I Identifier Name Formula
ASV DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL- D-VINYLGLYCINE C13 H21 N3 O6 S
FE2 FE (II) ION Fe
Citation: Crystallographic Studies on the Binding of Selectively Deuterated Lld- and Lll-Substrate Epimers by Isopenicillin N Synthase.
(2010) Biochem.Biophys.Res.Commun.
Isopenicillin N synthase (IPNS) is a non-heme iron(II) oxidase which catalyses the biosynthesis of isopenicillin N (IPN) from the tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine (lll-ACV). Herein we report crystallographic studies to investigate the binding of a truncated lll-substrate in the active site of IPNS. Two epimeric tripeptides have been prepared by solution phase peptide synthesis and crystallised with the enzyme. delta-l-alpha-Aminoadipoyl-l-cysteinyl-d-2-amino-3,3-dideuteriobutyrate (lll-ACd(2)Ab) has the same configuration as the natural substrate lld-ACV at each of its three stereocentres; its epimer delta-l-alpha-aminoadipoyl-l-cysteinyl-l-2-amino-3,3-dideuteriobutyrate (lll-ACd(2)Ab) has the opposite configuration at its third amino acid. lll-ACV has previously been shown to inhibit IPNS turnover of its substrate lld-ACV; the all-protiated tripeptide delta-l-alpha-aminoadipoyl-l-cysteinyl-d-2-aminobutyrate (lld-ACAb) is a substrate for IPNS, being turned over to a mixture of penam and cepham products. Comparisons between the crystal structures of the IPNS:Fe(II):lld-ACd(2)Ab and IPNS:Fe(II):lll-ACd(2)Ab offer a possible rationale for the previously observed inhibitory effects of lll-ACV on IPNS activity.
Molecular Description Classification : Oxidoreductase
Structure Weight: 37967.43
Molecule : ISOPENICILLIN N SYNTHASE
Polymer : 1
Type : polypeptide(L) Length: 331
Chains : A
EC# : 1.21.3.1 Go to IUBMB EC entry
