PDBsum entry 2pq2

Hydrolase

PDB id: 2pq2

Contents

Protein chain

279 a.a. *

Ligands

GLY-ALA-LEU-ALA-GLY

NO3

Metals

_CA

Waters ×263

* Residue conservation analysis

PDB id:

2pq2

Name:

Hydrolase

Title:

Structure of serine proteinase k complex with a highly flexible hydrophobic peptide at 1.8a resolution

Structure:

Proteinase k. Chain: a. Synonym: tritirachium alkaline proteinase, endopeptidase k. Mutation: yes. Galag peptide. Chain: b. Engineered: yes

Source:

Engyodontium album. Organism_taxid: 37998. Strain: fungi. Synthetic: yes. Other_details: peptide

Resolution:

1.82Å R-factor: 0.170 R-free: 0.207

Authors:

A.S.Ethayathulla,A.K.Singh,N.Singh,S.Sharma,M.Sinha,R.K.Somvanshi, P.Kaur,S.Dey,A.Srinivasan,T.P.Singh

Key ref:

A.S.Ethayathulla et al. Structure of serine proteinase k complex with a highly flexible hydrophobic peptide at 1.8a resolution. To be published, .

Date:

01-May-07 Release date: 29-May-07

Protein chain

P0DP29  (CALM1_RAT) -  Calmodulin-1 from Rattus norvegicus

Seq: 149 a.a.

Struc: 279 a.a.*

* PDB and UniProt seqs differ at 122 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.21.64 - peptidase K.
• Reaction: Hydrolysis of keratin and of other proteins, with subtilisin-like specificity. Hydrolyzes peptides amides.