PDBsum entry 2xu3

Hydrolase

PDB id

2xu3

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Contents

			Protein chain

					220 a.a. *

			Ligands

					XU3


					BTB ×2

			Metals

					_CL

			Waters ×373

* Residue conservation analysis

PDB id:

2xu3

Links

Name:

Hydrolase

Title:

Cathepsin l with a nitrile inhibitor

Structure:

Cathepsin l1. Chain: a. Fragment: catalytic domain, residues 114-333. Synonym: major excreted protein, mep. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

0.90Å

R-factor:

0.142

R-free:

0.155

Authors:

D.W.Banner,J.M.Benz,W.Haap

Key ref:

L.A.Hardegger et al. (2011). Systematic investigation of halogen bonding in protein-ligand interactions. Angew Chem Int Ed Engl, 50, 314-318. PubMed id: 21184410

Date:

14-Oct-10

Release date:

12-Jan-11

PROCHECK

	Headers

	References

Protein chain

P07711 (CATL1_HUMAN) - Procathepsin L from Homo sapiens

Seq: Struc:					333 a.a. 220 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.4.22.15 - cathepsin L.

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

Reaction:

Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.

	Angew Chem Int Ed Engl 50:314-318 (2011)
PubMed id: 21184410

Systematic investigation of halogen bonding in protein-ligand interactions.
L.A.Hardegger, B.Kuhn, B.Spinnler, L.Anselm, R.Ecabert, M.Stihle, B.Gsell, R.Thoma, J.Diez, J.Benz, J.M.Plancher, G.Hartmann, D.W.Banner, W.Haap, F.Diederich.

ABSTRACT

No abstract given.