PDBsum entry 5u3a

Hydrolase

PDB id

5u3a

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Contents

			Protein chain

					496 a.a.

			Ligands

					NAG

			Metals

					_CA


					_CL

			Waters ×601

PDB id:

5u3a

Links

Name:

Hydrolase

Title:

Ultra high resolution crystal structure of human pancreatic alpha amylase

Structure:

Pancreatic alpha-amylase. Chain: a. Synonym: pa,1,4-alpha-d-glucan glucanohydrolase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Organ: pancreas. Gene: amy2a. Expressed in: komagataella pastoris. Expression_system_taxid: 4922

Resolution:

0.95Å

R-factor:

0.110

R-free:

0.121

Authors:

S.Caner,G.D.Brayer

Key ref:

L.Goldbach et al. (2019). Folding Then Binding vs Folding Through Binding in Macrocyclic Peptide Inhibitors of Human Pancreatic α-Amylase. ACS Chem Biol, 14, 1751-1759. PubMed id: 31241898 DOI: 10.1021/acschembio.9b00290

Date:

01-Dec-16

Release date:

06-Dec-17

PROCHECK

	Headers

	References

Protein chain

P04746 (AMYP_HUMAN) - Pancreatic alpha-amylase from Homo sapiens

Seq: Struc:					511 a.a. 496 a.a.*

Key:

PfamA domain

Secondary structure

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



		Enzyme reactions

Enzyme class:

E.C.3.2.1.1 - alpha-amylase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.

DOI no: 10.1021/acschembio.9b00290	ACS Chem Biol 14:1751-1759 (2019)
PubMed id: 31241898

Folding Then Binding vs Folding Through Binding in Macrocyclic Peptide Inhibitors of Human Pancreatic α-Amylase.
L.Goldbach, B.J.A.Vermeulen, S.Caner, M.Liu, C.Tysoe, L.van Gijzel, R.Yoshisada, M.Trellet, H.van Ingen, G.D.Brayer, A.M.J.J.Bonvin, S.A.K.Jongkees.

ABSTRACT

De novo macrocyclic peptides, derived using selection technologies such as phage and mRNA display, present unique and unexpected solutions to challenging biological problems. This is due in part to their unusual folds, which are able to present side chains in ways not available to canonical structures such as α-helices and β-sheets. Despite much recent interest in these molecules, their folding and binding behavior remains poorly characterized. In this work, we present cocrystallization, docking, and solution NMR structures of three de novo macrocyclic peptides that all bind as competitive inhibitors with single-digit nanomolar K