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PDBsum entry 4zkl

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
4zkl

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
112 a.a.
Ligands
AMP-JB6
AMP
Waters ×194
PDB id:
4zkl
Name: Hydrolase
Title: Crystal structure of human histidine triad nucleotide-binding protein 1 (hhint1) complexed with jb419 (ap4a analog)
Structure: Histidine triad nucleotide-binding protein 1. Chain: a, b, c, d. Fragment: unp residues 1-126. Synonym: adenosine 5'-monophosphoramidase,protein kinasE C inhibitor 1,protein kinasE C-interacting protein 1,pkci-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hint1, hint, pkci1, prkcnh1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.34Å     R-factor:   0.189     R-free:   0.239
Authors: R.M.Dolot,R.Kaczmarek,A.Seda,A.Krakowiak,J.Baraniak,B.Nawrot
Key ref: R.Dolot et al. (2016). Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of Ap4A. Int J Biol Macromol, 87, 62-69. PubMed id: 26905466 DOI: 10.1016/j.ijbiomac.2016.02.047
Date:
30-Apr-15     Release date:   02-Mar-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P49773  (HINT1_HUMAN) -  Adenosine 5'-monophosphoramidase HINT1 from Homo sapiens
Seq:
Struc:
126 a.a.
112 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.3.4.22.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 3: E.C.3.9.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
DOI no: 10.1016/j.ijbiomac.2016.02.047 Int J Biol Macromol 87:62-69 (2016)
PubMed id: 26905466  
 
 
Crystallographic studies of the complex of human HINT1 protein with a non-hydrolyzable analog of Ap4A.
R.Dolot, R.Kaczmarek, A.Sęda, A.Krakowiak, J.Baraniak, B.Nawrot.
 
  ABSTRACT  
 
No abstract given.

 

 

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