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PDBsum entry 3n4i

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protein Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
3n4i

 

 

 

 

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Contents
Protein chains
265 a.a.
165 a.a.
Waters ×362
PDB id:
3n4i
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of the shv-1 d104e beta-lactamase/beta-lactamase inhibitor protein (blip) complex
Structure: Beta-lactamase shv-1. Chain: a. Synonym: pit-2. Engineered: yes. Mutation: yes. Beta-lactamase inhibitory protein. Chain: b. Synonym: blip. Engineered: yes
Source: Klebsiella pneumoniae. Organism_taxid: 573. Gene: bla, bla shv1, rsmk03643, rsmk03800, shv1. Expressed in: escherichia coli. Expression_system_taxid: 562. Streptomyces clavuligerus. Organism_taxid: 1901. Gene: bli. Expression_system_taxid: 469008.
Resolution:
1.56Å     R-factor:   0.171     R-free:   0.179
Authors: M.S.Hanes,K.A.Reynolds,C.Mcnamara,P.Ghosh,R.A.Bonomo,J.F.Kirsch, T.M.Handel
Key ref: M.S.Hanes et al. (2011). Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions. Proteins, 79, 1267-1276. PubMed id: 21294157
Date:
21-May-10     Release date:   09-Mar-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AD64  (BLA1_KLEPN) -  Beta-lactamase SHV-1 from Klebsiella pneumoniae
Seq:
Struc:
286 a.a.
265 a.a.*
Protein chain
Pfam   ArchSchema ?
P35804  (BLIP_STRCL) -  Beta-lactamase inhibitory protein from Streptomyces clavuligerus
Seq:
Struc:
201 a.a.
165 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.5.2.6  - beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Penicillin Biosynthesis and Metabolism
      Reaction: a beta-lactam + H2O = a substituted beta-amino acid
      Cofactor: Zn(2+)

 

 
Proteins 79:1267-1276 (2011)
PubMed id: 21294157  
 
 
Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions.
M.S.Hanes, K.A.Reynolds, C.McNamara, P.Ghosh, R.A.Bonomo, J.F.Kirsch, T.M.Handel.
 
  ABSTRACT  
 
No abstract given.

 

 

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