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1X0J

Crystal structure analysis of the N-terminal bromodomain of human Brd2

Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DTT A 1301
ChainResidue
AVAL103
ALEU108
ATYR113
AASN156
AILE162
AHOH1303

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTT B 1302
ChainResidue
BILE162
BHOH1306
BHOH1345
BHOH1398
BLEU108
BTYR113
BASN156

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DTT C 1303
ChainResidue
BGLN80
CPRO98
CVAL103
CLEU108
CASN156
CILE162
CHOH1403
CHOH1417

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES C 1401
ChainResidue
ATRP97
AARG100
CARG128
CASN132
CTYR134
CHOH1484

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues60
DetailsBROMODOMAIN_1 Bromodomain signature. AwpFrqpvDavklglpDYHkiIkqpMdmgtIkrrlenny..Ywaasecmqdfnt.MftNCyiY
ChainResidueDetails
AALA96-TYR155

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:37731000, ECO:0007744|PDB:8SB6
ChainResidueDetails
AASP112
CTYR155
CASN156
CLYS157
ATYR155
AASN156
ALYS157
BASP112
BTYR155
BASN156
BLYS157
CASP112

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20048151, ECO:0007744|PDB:2DVQ, ECO:0007744|PDB:2DVS
ChainResidueDetails
AASP160
AASP161
BASP160
BASP161
CASP160
CASP161

226707

PDB entries from 2024-10-30

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