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3HMF

Crystal Structure of the second Bromodomain of Human Poly-bromodomain containing protein 1 (PB1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0016586cellular_componentRSC-type complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS246
AHIS289
ACL293
ACL294

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 2
ChainResidue
AGLU184
AGLU187
AHIS290
AGLU291

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 292
ChainResidue
ATYR281
ALYS284
ALYS284
AALA285
AGLU288
ACL293
AHOH321
AHOH10

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 293
ChainResidue
AZN1
AHIS246
ALYS284
AHIS289
AEDO292

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 294
ChainResidue
AZN1
AHIS246
AHIS289

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. SelFqklpSkvqyp..DYYaiIkepIdlktIaqriqngs..Yksihamakdidl.LakNAktY
ChainResidueDetails
ASER205-TYR262

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER178

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS210

218853

PDB entries from 2024-04-24

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