PDBsum entry 3url

Hydrolase/hydrolase inhibitor

PDB id: 3url

Contents

Protein chain

329 a.a.

Ligands

HIS-SER-LEU-PHE-HIS-PUK-THR-PRO

SO4 ×3

Waters ×317

PDB id:

3url

Name:

Hydrolase/hydrolase inhibitor

Title:

Endothiapepsin-db6 complex.

Structure:

Endothiapepsin. Chain: a. Fragment: unp residues 90-419. Synonym: aspartate protease. Db6 peptide. Chain: b. Engineered: yes

Source:

Endothia parasitica. Chesnut blight fungus. Organism_taxid: 5116. Synthetic: yes

Resolution:

2.00Å R-factor: 0.147 R-free: 0.237

Authors:

D.Bailey,J.Sanz-Aparicio,A.Albert,J.B.Cooper

Key ref:

D.Bailey et al. (2012). An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases. Acta Crystallogr D Biol Crystallogr, 68, 541-552. PubMed id: 22525752

Date:

22-Nov-11 Release date: 18-Apr-12

Protein chain

P11838  (CARP_CRYPA) -  Endothiapepsin from Cryphonectria parasitica

Seq: 419 a.a.

Struc: 329 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.23.22 - endothiapepsin.
• Reaction: Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk.

Acta Crystallogr D Biol Crystallogr 68:541-552 (2012)

PubMed id: 22525752

An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases.

D.Bailey, E.P.Carpenter, A.Coker, S.Coker, J.Read, A.T.Jones, P.Erskine, C.F.Aguilar, M.Badasso, L.Toldo, F.Rippmann, J.Sanz-Aparicio, A.Albert, T.L.Blundell, N.B.Roberts, S.P.Wood, J.B.Cooper.

ABSTRACT

No abstract given.