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PDBsum entry 4ijd

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
4ijd

 

 

 

 

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Contents
Protein chain
215 a.a.
Ligands
UNX ×24
Metals
_ZN ×4
Waters ×60
PDB id:
4ijd
Name: Transferase
Title: Crystal structure of methyltransferase domain of human pr domain- containing protein 9
Structure: Histone-lysine n-methyltransferase prdm9. Chain: a, b. Fragment: unp residues 195-415. Synonym: pr domain zinc finger protein 9, pr domain-containing protein 9. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: prdm9, pfm6. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.15Å     R-factor:   0.199     R-free:   0.264
Authors: A.Dong,L.Dombrovski,Y.Li,W.Tempel,C.Bountra,C.H.Arrowsmith, A.M.Edwards,P.J.Brown,H.Wu,Structural Genomics Consortium (Sgc)
Key ref: L.Dombrovski et al. Crystal structure of methyltransferase domain of huma domain-Containing protein 9. To be published, .
Date:
21-Dec-12     Release date:   13-Feb-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Q9NQV7  (PRDM9_HUMAN) -  Histone-lysine N-methyltransferase PRDM9 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
894 a.a.
215 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.2.1.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: E.C.2.1.1.354  - [histone H3]-lysine(4) N-trimethyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl4-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6- trimethyl-L-lysyl4-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
L-lysyl(4)-[histone H3]
+ 3 × S-adenosyl-L-methionine
= N(6),N(6),N(6)- trimethyl-L-lysyl(4)-[histone H3]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
   Enzyme class 3: E.C.2.1.1.355  - [histone H3]-lysine(9) N-trimethyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6- trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
L-lysyl(9)-[histone H3]
+ 3 × S-adenosyl-L-methionine
= N(6),N(6),N(6)- trimethyl-L-lysyl(9)-[histone H3]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
   Enzyme class 4: E.C.2.1.1.359  - [histone H3]-lysine(36) N-trimethyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl36-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6- trimethyl-L-lysyl36-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
L-lysyl(36)-[histone H3]
+ 3 × S-adenosyl-L-methionine
= N(6),N(6),N(6)- trimethyl-L-lysyl(36)-[histone H3]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
   Enzyme class 5: E.C.2.1.1.361  - [histone H4]-lysine(20) N-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl20-[histone H4] + S-adenosyl-L-methionine = N6-methyl-L- lysyl20-[histone H4] + S-adenosyl-L-homocysteine + H+
L-lysyl(20)-[histone H4]
+ 3 × S-adenosyl-L-methionine
= N(6)-methyl-L- lysyl(20)-[histone H4]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
   Enzyme class 6: E.C.2.1.1.362  - [histone H4]-N-methyl-L-lysine(20) N-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6-methyl-L-lysyl20-[histone H4] + S-adenosyl-L-methionine = N6,N6-dimethyl-L-lysyl20-[histone H4] + S-adenosyl-L-homocysteine + H+
N(6)-methyl-L-lysyl(20)-[histone H4]
+ 3 × S-adenosyl-L-methionine
= N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4]
+ 3 × S-adenosyl-L-homocysteine
+ 3 × H(+)
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.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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