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PDBsum entry 3u3r

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protein ligands links
Transferase PDB id
3u3r

 

 

 

 

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Contents
Protein chain
288 a.a.
Ligands
NPO ×2
A3P
Waters ×100
PDB id:
3u3r
Name: Transferase
Title: Crystal structure of d249g mutated human sult1a1 bound to pap and p- nitrophenol
Structure: Sulfotransferase 1a1. Chain: a. Fragment: unp residues 1-295. Synonym: st1a1, aryl sulfotransferase 1, hast1/hast2, phenol sulfotransferase 1, phenol-sulfating phenol sulfotransferase 1, p-pst 1, st1a3, thermostable phenol sulfotransferase, ts-pst. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: homo sapiens. Gene: hsult1a1 d249g mutation, ok/sw-cl.88, stp, stp1, sult1a1. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.36Å     R-factor:   0.170     R-free:   0.217
Authors: C.Guttman,I.Berger,A.Aharoni,R.Zarivach
Key ref: I.Berger et al. (2011). The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. Plos One, 6, e26794. PubMed id: 22069470
Date:
06-Oct-11     Release date:   16-Nov-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P50225  (ST1A1_HUMAN) -  Sulfotransferase 1A1 from Homo sapiens
Seq:
Struc:
295 a.a.
288 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.2.8.2.1  - aryl sulfotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a phenol + 3'-phosphoadenylyl sulfate = an aryl sulfate + adenosine 3',5'-bisphosphate + H+
phenol
+
3'-phosphoadenylyl sulfate
Bound ligand (Het Group name = NPO)
matches with 70.00% similarity
=
aryl sulfate
Bound ligand (Het Group name = A3P)
corresponds exactly
+ adenosine 3',5'-bisphosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Plos One 6:e26794 (2011)
PubMed id: 22069470  
 
 
The molecular basis for the broad substrate specificity of human sulfotransferase 1A1.
I.Berger, C.Guttman, D.Amar, R.Zarivach, A.Aharoni.
 
  ABSTRACT  
 
No abstract given.

 

 

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