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protein ligands metals links
Transferase PDB id
2p3s
Jmol
Contents
Protein chain
216 a.a. *
Ligands
AP5
Metals
_ZN
_MG
Waters ×275
* Residue conservation analysis
PDB id:
2p3s
Name: Transferase
Title: Crystal structure of a thermostable mutant of bacillus subtilis adenylate kinase (g214r/q199r)
Structure: Adenylate kinase. Chain: a. Synonym: atp-amp transphosphorylase, ak, superoxide- inducible protein 16, soi16. Engineered: yes. Mutation: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: 168. Gene: adk. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.80Å     R-factor:   0.198     R-free:   0.239
Authors: R.Counago,C.J.Wilson,J.Myers,G.Wu,Y.Shamoo
Key ref: R.Counago et al. Crystal structure of a thermostable mutant of bacillus subtilis adenylate kinase (g214r/q199r). To be published,
Date:
09-Mar-07     Release date:   22-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16304  (KAD_BACSU) -  Adenylate kinase
Seq:
Struc: 		217 a.a.
216 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.7.4.3  - Adenylate kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + AMP = 2 ADP
ATP
Bound ligand (Het Group name = AP5)
matches with 54.00% similarity 		+ AMP
 = 2 × ADP
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     nucleobase, nucleoside, nucleotide and nucleic acid metabolic process   2 terms 
  Biochemical function     nucleotide binding     9 terms