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Ligands
Code Name Style Show Link
Non-standard Residues
Code Name Show
MLZ N-methyl-lysine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 2B2V   PDBj   RCSB PDB   PDBe
Header : PEPTIDE BINDING PROTEIN
Title : Crystal structure analysis of human CHD1 chromodomains 1 and 2 bound to histone H3 resi 1-15 MeK4
Release Data : 2005-12-27
Compound :
mol_id molecule chains synonym
1 Chromodomain-helicase-DNA-binding protein 1 A,B CHD-1
fragment: residues 268-443
mol_id molecule chains synonym
2 Chromodomain-helicase-DNA-binding protein 1 C CHD-1
fragment: residues 268-373
mol_id molecule chains
3 Histone H3 D
fragment: residues 1-15
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CHD1
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET11a
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: CHD1
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET11a
mol_id organism_scientific
3
synthetic: yes
other_details: This sequence occurs naturally in Homo sapiens (Humans).
Authors : Flanagan IV, J.F., Mi, L.-Z., Chruszcz, M., Cymborowski, M., Clines, K.L., Kim, Y., Minor, W., Rastinejad, F., Khorasanizadeh, S.
Keywords : CHD, Chromodomain, three stranded antiparallel Beta sheet, alpha helix linker, histone H3, monomethyllysine, PEPTIDE BINDING PROTEIN
Exp. method : X-RAY DIFFRACTION ( 2.65 Å )
Citation :

Double chromodomains cooperate to recognize the methylated histone H3 tail.

Flanagan, J.F.,Mi, L.Z.,Chruszcz, M.  et al.
(2005)  Nature  438 : 1181 - 1185

PubMed: 16372014
DOI: 10.1038/nature04290

Chain : C
UniProt : O14646 (CHD1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + H2O = ADP + H(+) + phosphate 3.6.4.12 -
-
Chain : D
UniProt : P68431 (H31_HUMAN)
Reaction : -