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5PNZ

PanDDA analysis group deposition -- Crystal Structure of BRD1 in complex with N10162a

Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue EDO A 201
ChainResidue
AASN110
AEDO202
AHOH359

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 202
ChainResidue
AHOH306
AHOH313
AILE54
AVAL59
ACYS106
APHE116
AEDO201
AHOH301

site_idAC3
Number of Residues6
Detailsbinding site for residue NA B 201
ChainResidue
ALYS108
AHOH342
AHOH368
BMET107
BASN110
BTYR117

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 202
ChainResidue
BILE54
BASN110
BHOH301
BHOH306

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO B 203
ChainResidue
BLEU92
BGLU96
BLEU131
BARG135
BHOH312

site_idAC6
Number of Residues9
Detailsbinding site for residue EDO B 204
ChainResidue
BTHR36
BLEU84
BGLN87
BGLY88
BTYR89
B8S4205
BHOH348
BHOH353
BHOH402

site_idAC7
Number of Residues16
Detailsbinding site for residue 8S4 B 205
ChainResidue
BMET28
BARG31
BLEU35
BPRO51
BLYS90
BASN91
BLEU143
BGLU144
BEDO204
BHOH307
BHOH326
BHOH348
BHOH384
BHOH400
BHOH412
BHOH433

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
ALYS62
BLYS62

222926

PDB entries from 2024-07-24

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