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5PR2

PanDDA analysis group deposition -- Crystal Structure of BRD1 after initial refinement with no ligand modelled (structure 75)

Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 201
ChainResidue
ALYS108
AHOH325
AHOH343
BMET107
BASN110

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 202
ChainResidue
AASN110
AEDO203

site_idAC3
Number of Residues9
Detailsbinding site for residue EDO A 203
ChainResidue
AVAL59
ACYS106
APHE116
AEDO202
AHOH302
AHOH303
AHOH306
AILE54
APHE55

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 201
ChainResidue
BILE54
BASN110
BHOH301
BHOH321
BHOH385

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 202
ChainResidue
BLEU92
BGLU96
BLEU131
BARG135
BHOH304

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. AriFaqpvSlkevp..DYLdhIkhpMdfatMrkrleaqg..Yknlhefeedfdl.IidNCmkY
ChainResidueDetails
AALA52-TYR109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS62
ALYS62

219869

PDB entries from 2024-05-15

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