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PDBsum entry 2kyu
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Transferase
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Title:
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The solution structure of the phd3 finger of mll
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Structure:
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Histone-lysine n-methyltransferase mll. Chain: a. Fragment: phd3 finger (unp residues 1564-1628). Synonym: zinc finger protein hrx, all-1, trithorax-like protein, lysine n-methyltransferase 2a, kmt2a, cxxc-type zinc finger protein 7. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mll, all1, cxxc7, hrx, htrx, kmt2a, mll1, trx1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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10 models
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Authors:
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S.Park,J.H.Bushweller
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Key ref:
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S.Park
et al.
(2010).
The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression .
Biochemistry,
49,
6576-6586.
PubMed id:
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Date:
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08-Jun-10
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Release date:
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25-Aug-10
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PROCHECK
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Headers
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References
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Q03164
(KMT2A_HUMAN) -
Histone-lysine N-methyltransferase 2A from Homo sapiens
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Seq:
Struc:
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3969 a.a.
67 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.1.1.-
- ?????
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Enzyme class 2:
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E.C.2.1.1.364
- [histone H3]-lysine(4) N-methyltransferase.
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Reaction:
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L-lysyl4-[histone H3] + S-adenosyl-L-methionine = N6-methyl-L- lysyl4-[histone H3] + S-adenosyl-L-homocysteine + H+
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L-lysyl(4)-[histone H3]
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+
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S-adenosyl-L-methionine
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=
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N(6)-methyl-L- lysyl(4)-[histone H3]
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+
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S-adenosyl-L-homocysteine
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+
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H(+)
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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.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Biochemistry
49:6576-6586
(2010)
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PubMed id:
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The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression .
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S.Park,
U.Osmers,
G.Raman,
R.H.Schwantes,
M.O.Diaz,
J.H.Bushweller.
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ABSTRACT
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Links
