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6HT1

Crystal structure of MLLT1 (ENL) YEATS domain in complexed with SGC-iMLLT (compound 92)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 A 201
ChainResidue
ALYS50
AARG63
AVAL65
ALYS67

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 202
ChainResidue
AARG10
AARG16
ALYS121

site_idAC3
Number of Residues8
Detailsbinding site for residue EDO A 203
ChainResidue
ACYS42
AILE44
APHE47
AALA138
AGLY139
AHOH302
AVAL9
AARG10

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 204
ChainResidue
APHE100
ATHR101
AASN111
AARG118

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 205
ChainResidue
AGLU93
AGLU94

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 206
ChainResidue
AARG16
AGLN18
ATRP32

site_idAC7
Number of Residues5
Detailsbinding site for residue EDO A 207
ChainResidue
AVAL98
ATHR123
AHOH307
AHOH316
AHOH332

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO A 208
ChainResidue
APHE81
AASP103
ALEU104
AHOH331

site_idAC9
Number of Residues4
Detailsbinding site for residue EDO A 209
ChainResidue
AASN3
AASP31
AGLU75
ASER76

site_idAD1
Number of Residues13
Detailsbinding site for residue GQ5 A 210
ChainResidue
AASN3
APHE28
AHIS56
ASER58
APHE59
APRO60
AGLU75
ASER76
AGLY77
ATYR78
AALA79
AGLY80
AHOH315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Acylated histone binding => ECO:0000269|PubMed:28241141, ECO:0007744|PDB:5J9S
ChainResidueDetails
AASP103

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

217705

數據於2024-03-27公開中

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