General information
PDB ID 1MDY
Title CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION
PDB header TRANSCRIPTION/DNA
Date 1994-06-09
Experimental method X-RAY DIFFRACTION
Resolution (A) 2.8
Kind dna
Organism MUS MUSCULUS
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PDB PDBe MMDB Jena OCA
CATH PDBsum HSSP PDBePISA UniProt
ProteopediA BIPA
Composition of PDB entry and biounits
File: Protein chains: DNA chains: RNA chains: No. of models: Action:
PDB entry:
pdb1mdy.pdb ABCD EFGH 0
Biounits:
1mdy.pdb1.pdb AB EF 1
1mdy.pdb2.pdb CD GH 1
Pfam domains
Name: Type: Domain: E-value: Significance: Clan: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
HLH Domain P10085_110-161 4.4e-14 1 No_clan A 110 161 EF  H-Bb H-Mj 
HLH Domain P10085_110-161 3.2e-14 1 No_clan B 110 161 EF  H-Bb H-Mj L-Bb 
HLH Domain P10085_110-161 3.2e-14 1 No_clan C 110 161 GH  H-Bb H-Mj 
HLH Domain P10085_110-161 3.2e-14 1 No_clan D 110 161 GH  H-Bb H-Mj 
SCOP domains
Classification: Protein: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
Class: All alpha proteins
  Fold: HLH-like
    Superfamily: HLH, helix-loop-helix DNA-binding domain
      Family: HLH, helix-loop-helix DNA-binding domain
Myod B/HLH domain A N/A N/A EF  H-Bb H-Mj 
Class: All alpha proteins
  Fold: HLH-like
    Superfamily: HLH, helix-loop-helix DNA-binding domain
      Family: HLH, helix-loop-helix DNA-binding domain
Myod B/HLH domain B N/A N/A EF  H-Bb H-Mj L-Bb 
Class: All alpha proteins
  Fold: HLH-like
    Superfamily: HLH, helix-loop-helix DNA-binding domain
      Family: HLH, helix-loop-helix DNA-binding domain
Myod B/HLH domain C N/A N/A GH  H-Bb H-Mj 
Class: All alpha proteins
  Fold: HLH-like
    Superfamily: HLH, helix-loop-helix DNA-binding domain
      Family: HLH, helix-loop-helix DNA-binding domain
Myod B/HLH domain D N/A N/A GH  H-Bb H-Mj 
GO terms
Protein chains: GO type: GO description:
A=102-166, B/C/D=105-166 C cytoplasm
A=102-166, B/C/D=105-166 C myofibril
A=102-166, B/C/D=105-166 C nuclear chromatin
A=102-166, B/C/D=105-166 C nuclear euchromatin
A=102-166, B/C/D=105-166 C nucleoplasm
A=102-166, B/C/D=105-166 C nucleus
A=102-166, B/C/D=105-166 C transcription regulator complex
A=102-166, B/C/D=105-166 F chromatin binding
A=102-166, B/C/D=105-166 F chromatin DNA binding
A=102-166, B/C/D=105-166 F cis-regulatory region sequence-specific DNA binding
A=102-166, B/C/D=105-166 F DNA-binding transcription activator activity, RNA polymerase II-specific
A=102-166, B/C/D=105-166 F DNA-binding transcription factor activity
A=102-166, B/C/D=105-166 F DNA-binding transcription factor activity, RNA polymerase II-specific
A=102-166, B/C/D=105-166 F E-box binding
A=102-166, B/C/D=105-166 F enzyme binding
A=102-166, B/C/D=105-166 F nuclear hormone receptor binding
A=102-166, B/C/D=105-166 F promoter-specific chromatin binding
A=102-166, B/C/D=105-166 F protein homodimerization activity
A=102-166, B/C/D=105-166 F RNA polymerase II activating transcription factor binding
A=102-166, B/C/D=105-166 F RNA polymerase II cis-regulatory region sequence-specific DNA binding
A=102-166, B/C/D=105-166 F RNA polymerase II transcription regulatory region sequence-specific DNA binding
A=102-166, B/C/D=105-166 F sequence-specific DNA binding
A=102-166, B/C/D=105-166 F sequence-specific double-stranded DNA binding
A=102-166, B/C/D=105-166 F transcription factor binding
A=102-166, B/C/D=105-166 F ubiquitin protein ligase binding
A=102-166, B/C/D=105-166 P cardiac muscle cell differentiation
A=102-166, B/C/D=105-166 P cellular response to estradiol stimulus
A=102-166, B/C/D=105-166 P cellular response to glucocorticoid stimulus
A=102-166, B/C/D=105-166 P cellular response to oxygen levels
A=102-166, B/C/D=105-166 P cellular response to starvation
A=102-166, B/C/D=105-166 P cellular response to tumor necrosis factor
A=102-166, B/C/D=105-166 P histone H3 acetylation
A=102-166, B/C/D=105-166 P histone H4 acetylation
A=102-166, B/C/D=105-166 P muscle organ development
A=102-166, B/C/D=105-166 P myoblast differentiation
A=102-166, B/C/D=105-166 P myoblast fate determination
A=102-166, B/C/D=105-166 P myoblast fusion
A=102-166, B/C/D=105-166 P myotube cell development
A=102-166, B/C/D=105-166 P myotube differentiation
A=102-166, B/C/D=105-166 P myotube differentiation involved in skeletal muscle regeneration
A=102-166, B/C/D=105-166 P negative regulation of myoblast proliferation
A=102-166, B/C/D=105-166 P positive regulation of muscle cell differentiation
A=102-166, B/C/D=105-166 P positive regulation of myoblast differentiation
A=102-166, B/C/D=105-166 P positive regulation of myoblast fusion
A=102-166, B/C/D=105-166 P positive regulation of skeletal muscle fiber development
A=102-166, B/C/D=105-166 P positive regulation of skeletal muscle tissue regeneration
A=102-166, B/C/D=105-166 P positive regulation of snRNA transcription by RNA polymerase II
A=102-166, B/C/D=105-166 P positive regulation of transcription by RNA polymerase II
A=102-166, B/C/D=105-166 P positive regulation of transcription, DNA-templated
A=102-166, B/C/D=105-166 P regulation of alternative mRNA splicing, via spliceosome
A=102-166, B/C/D=105-166 P regulation of gene expression
A=102-166, B/C/D=105-166 P regulation of RNA splicing
A=102-166, B/C/D=105-166 P regulation of transcription by RNA polymerase II
A=102-166, B/C/D=105-166 P skeletal muscle cell differentiation
A=102-166, B/C/D=105-166 P skeletal muscle fiber adaptation
A=102-166, B/C/D=105-166 P skeletal muscle fiber development
A=102-166, B/C/D=105-166 P skeletal muscle tissue development
A=102-166, B/C/D=105-166 P skeletal muscle tissue regeneration
A=102-166, B/C/D=105-166 P striated muscle cell differentiation
Sequences
Download file with secondary structure created by Stride  
1mdy.pdb1.pdb:   [ download sequences in FASTA format ]
E (dna): 
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F (dna): 
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A (protein): 
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B (protein): 
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1mdy.pdb2.pdb:   [ download sequences in FASTA format ]
G (dna): 
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H (dna): 
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C (protein): 
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D (protein): 
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