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PDBsum entry 5n4v

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protein ligands links
Transferase PDB id
5n4v

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
273 a.a.
Ligands
ARG-LYS-ARG-ARG-
ARG-HIS-PRO-SER-
GLY
8MW
GOL
Waters ×158
PDB id:
5n4v
Name: Transferase
Title: Crystal structure of human pim-1 kinase in complex with a consensuspeptide and fragment like molekule 2-cyclopropyl-4,5- dimethylthieno[5,4-d]pyrimidine-6-carboxylic acid
Structure: Serine/threonine-protein kinase pim-1. Chain: a. Engineered: yes. Mutation: yes. Other_details: isofrom 2 of pim-1 kinase. Pimtide. Chain: d. Engineered: yes. Other_details: pim-1 consensus peptide
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: pim1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: plyss. Synthetic: yes. Organism_taxid: 9606
Resolution:
1.85Å     R-factor:   0.165     R-free:   0.187
Authors: C.Siefker,A.Heine,G.Klebe
Key ref: C.Siefker et al. A crystallographic fragment study with human pim-1 ki. To be published, .
Date:
11-Feb-17     Release date:   28-Feb-18    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P11309  (PIM1_HUMAN) -  Serine/threonine-protein kinase pim-1 from Homo sapiens
Seq:
Struc:
313 a.a.
273 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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