spacer
spacer

PDBsum entry 3cp7

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3cp7
Jmol
Contents
Protein chains
216 a.a. *
Ligands
FMT ×2
Waters ×657
* Residue conservation analysis
PDB id:
3cp7
Name: Hydrolase
Title: Crystal structure of a thermostable serine protease al20 from extremophilic microoganism
Structure: Alkaline serine protease al20. Chain: a, b. Ec: 3.4.21.1
Source: Nesterenkonia abyssinica
Resolution:
1.39Å     R-factor:   0.179     R-free:   0.199
Authors: N.Yang,J.Nan,X.-D.Su
Key ref:
N.Yang et al. (2008). Crystal structure of an alkaline serine protease from Nesterenkonia sp. defines a novel family of secreted bacterial proteases. Proteins, 73, 1072-1075. PubMed id: 18814301 DOI: 10.1002/prot.22233
Date:
31-Mar-08     Release date:   10-Feb-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
D0VWT7  (D0VWT7_9MICC) -  Alkaline serine protease AL20
Seq:
Struc:
218 a.a.
216 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.21.1  - Chymotrypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     2 terms  

 

 
DOI no: 10.1002/prot.22233 Proteins 73:1072-1075 (2008)
PubMed id: 18814301  
 
 
Crystal structure of an alkaline serine protease from Nesterenkonia sp. defines a novel family of secreted bacterial proteases.
N.Yang, J.Nan, E.Brostromer, R.Hatti-Kaul, X.D.Su.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Structure-based multiple sequence alignment of the NAALP family with representative members selected, see text for detailed names of each microorganism. The active site triad (S169, H41, and D91 as numbered in NAALPs) is labeled by filled squares, the oxyanion hole labeled by filled rings, and the two pairs of intramolecular disulfide bridges, C23-C42, C144-C162 were labeled by green numbers. The figure was produced by ESPript 2.2 (http://endscript.ibcp.fr/ESPript/ESPript/). (B) Topology diagram of the NAALP structure colored according to the secondary structure elements and different domains, with all helices red, and strands green (domain I) and yellow (domain II). (C) C trace of the NAALP dimer showing Mol A in yellow and Mol B in green, helices 1 and 3 forming the dimer interfaces predominantly. (D) Detailed C trace of Mol A of Figure 1D with the secondary structure elements numbered, the active site triad labeled as S169, H41, and D91 and the two pairs of intramolecular disulfide bridges labeled as C23-C42, C144-C162, with C atoms in yellow, N atoms in blue, O atoms in red, and S atoms in green. (E) 2Fo-Fc density maps of the active site of molecule A at 1.0 . The active triad is labeled as His41, Asp91, and Ser169, with C atoms in green, N atoms in blue, O atoms in red, and density map in light blue. The oxyanion hole formed by the main-chain NH groups of Gly167 and Ser169. A formic acid molecule is in the active sites, with C atom in yellow and O atoms in red.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2008, 73, 1072-1075) copyright 2008.