PDBsum entry 3k6z

Hydrolase

PDB id

3k6z

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Contents

			Protein chains

					198 a.a. *

			Waters ×482

* Residue conservation analysis

PDB id:

3k6z

Links

Name:

Hydrolase

Title:

Crystal structure of rv3671c protease, inactive form

Structure:

Possible membrane-associated serine protease. Chain: a, b. Fragment: unp residues 179-397. Synonym: serine protease. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Strain: h37rv. Gene: mt3772, rv3671c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.75Å

R-factor:

0.190

R-free:

0.239

Authors:

T.Biswas,J.Small,O.Vandal,S.Ehrt,O.V.Tsodikov

Key ref:

T.Biswas et al. (2010). Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress. Structure, 18, 1353-1363. PubMed id: 20947023

Date:

10-Oct-09

Release date:

13-Oct-10

PROCHECK

	Headers

	References

Protein chains

P9WHR9 (Y3671_MYCTU) - Serine protease Rv3671c from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: Struc:					397 a.a. 198 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.4.21.- - ?????

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

	Structure 18:1353-1363 (2010)
PubMed id: 20947023

Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.
T.Biswas, J.Small, O.Vandal, T.Odaira, H.Deng, S.Ehrt, O.V.Tsodikov.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

22868759

J.A.Bell, K.L.Ho, and R.Farid (2012).
Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.

Acta Crystallogr D Biol Crystallogr, 68, 935-952.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.