PDBsum entry 3nzj

Hydrolase/hydrolase inhibitor

PDB id: 3nzj

Contents

Protein chains

250 a.a. *

244 a.a. *

241 a.a. *

242 a.a. *

233 a.a. *

244 a.a. *

243 a.a. *

222 a.a. *

204 a.a. *

198 a.a. *

212 a.a. *

222 a.a. *

233 a.a. *

196 a.a. *

Ligands

BOC-TY5-ALA-TRO-ABN ×2

MES ×2

Waters ×1336

* Residue conservation analysis

PDB id:

3nzj

Name:

Hydrolase/hydrolase inhibitor

Title:

Crystal structure of yeast 20s proteasome in complex with ligand 2a

Structure:

Proteasome component y7. Chain: a, o. Synonym: macropain subunit y7, multicatalytic endopeptidase complex subunit y7, proteinase ysce subunit 7. Proteasome component y13. Chain: b, p. Synonym: macropain subunit y13, multicatalytic endopeptidase complex subunit y13, proteinase ysce subunit 13. Proteasome component pre6.

Source:

Saccharomyces cerevisiae. Brewer's yeast,lager beer yeast,yeast. Organism_taxid: 4932. Synthetic: yes

Resolution:

2.40Å R-factor: 0.233 R-free: 0.249

Authors:

M.Groll,N.Gallastegui,X.Marechal,V.Le Ravalec,N.Basse,N.Richy, E.Genin,R.Huber,M.Moroder,V.Vidal,M.Reboud-Ravaux

Key ref:

M.Groll et al. (2010). 20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A. Chemmedchem, 5, 1701-1705. PubMed id: 20715286

Date:

16-Jul-10 Release date: 16-Feb-11

Protein chains

P23639  (PSA2_YEAST) -  Proteasome subunit alpha type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 250 a.a.

Struc: 250 a.a.

Protein chains

P23638  (PSA3_YEAST) -  Proteasome subunit alpha type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 258 a.a.

Struc: 244 a.a.

Protein chains

P40303  (PSA4_YEAST) -  Proteasome subunit alpha type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 254 a.a.

Struc: 241 a.a.

Protein chains

P32379  (PSA5_YEAST) -  Proteasome subunit alpha type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 260 a.a.

Struc: 242 a.a.

Protein chains

P40302  (PSA6_YEAST) -  Proteasome subunit alpha type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 234 a.a.

Struc: 233 a.a.

Protein chains

P21242  (PSA7_YEAST) -  Probable proteasome subunit alpha type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 288 a.a.

Struc: 244 a.a.

Protein chains

P21243  (PSA1_YEAST) -  Proteasome subunit alpha type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 252 a.a.

Struc: 243 a.a.

Protein chains

P25043  (PSB2_YEAST) -  Proteasome subunit beta type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 261 a.a.

Struc: 222 a.a.

Protein chains

P25451  (PSB3_YEAST) -  Proteasome subunit beta type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 205 a.a.

Struc: 204 a.a.

Protein chains

P22141  (PSB4_YEAST) -  Proteasome subunit beta type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 198 a.a.

Struc: 198 a.a.

Protein chains

P30656  (PSB5_YEAST) -  Proteasome subunit beta type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 287 a.a.

Struc: 212 a.a.

Protein chains

P23724  (PSB6_YEAST) -  Proteasome subunit beta type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 241 a.a.

Struc: 222 a.a.

Protein chains

P30657  (PSB7_YEAST) -  Proteasome subunit beta type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 266 a.a.

Struc: 233 a.a.

Protein chains

P38624  (PSB1_YEAST) -  Proteasome subunit beta type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 215 a.a.

Struc: 196 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2: E.C.3.4.25.1 - proteasome endopeptidase complex.
• Reaction: Cleavage at peptide bonds with very broad specificity.

Chemmedchem 5:1701-1705 (2010)

PubMed id: 20715286

20S proteasome inhibition: designing noncovalent linear peptide mimics of the natural product TMC-95A.

M.Groll, N.Gallastegui, X.Maréchal, V.Le Ravalec, N.Basse, N.Richy, E.Genin, R.Huber, L.Moroder, J.Vidal, M.Reboud-Ravaux.

ABSTRACT

No abstract given.