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PDBsum entry 2f46

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2f46
Jmol
Contents
Protein chains
143 a.a. *
Ligands
UNL
Metals
_CL ×2
Waters ×411
* Residue conservation analysis
PDB id:
2f46
Name: Hydrolase
Title: Crystal structure of a putative phosphatase (nma1982) from n meningitidis z2491 at 1.41 a resolution
Structure: Hypothetical protein. Chain: a, b. Engineered: yes
Source: Neisseria meningitidis z2491. Organism_taxid: 122587. Strain: fam18. Gene: 7380613. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.41Å     R-factor:   0.201     R-free:   0.228
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
S.S.Krishna et al. (2007). Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases. Proteins, 69, 415-421. PubMed id: 17636569 DOI: 10.1002/prot.21314
Date:
22-Nov-05     Release date:   07-Feb-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A1KVD0  (A1KVD0_NEIMF) -  Uncharacterized protein
Seq:
Struc:
155 a.a.
143 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     1 term  

 

 
DOI no: 10.1002/prot.21314 Proteins 69:415-421 (2007)
PubMed id: 17636569  
 
 
Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases.
S.S.Krishna, L.Tautz, Q.Xu, D.McMullan, M.D.Miller, P.Abdubek, E.Ambing, T.Astakhova, H.L.Axelrod, D.Carlton, H.J.Chiu, T.Clayton, M.DiDonato, L.Duan, M.A.Elsliger, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, A.T.Morse, T.Mustelin, E.Nigoghossian, S.Oommachen, R.Reyes, C.L.Rife, H.van den Bedem, D.Weekes, A.White, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. Crystal structure of NMA1982: (A) Stereo ribbon diagram of NMA1982 monomer color-coded from N-terminus (blue) to C-terminus (red). Helices (H1-H6) and -strands ( 1- 5) are labeled. (B) Diagram showing the secondary structural elements superimposed on its primary sequence. The -helices, -strands of -sheet A, and -hairpin is depicted as a red loop. The disordered region is displayed as a broken line.
Figure 2.
Figure 2. Structural comparison of NMA1982 with other PTPs: (A) Multiple structural alignment of NMA1982 (grey), human kinase-associated phosphatase (1fpz; magenta), and putative phosphatase from Arabidopsis thaliana (1xri; lilac). Insertions specific to human and A. thaliana proteins are denoted by I[Hs] and I[At], respectively. Cys and Arg residues from the active site loop are shown in ball-and-stick. (B) Structural alignment of NMA1982 (grey) and the putative phosphatase from Arabidopsis thaliana (1xri; lilac). Cys and Arg residues from the active site loop are shown in ball-and-stick representation, and the residue numbers correspond to NMA1982.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 415-421) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20944204 A.Bateman, P.Coggill, and R.D.Finn (2010).
DUFs: families in search of function.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1148-1152.  
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