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3TLP

Crystal structure of the fourth bromodomain of human poly-bromodomain containing protein 1 (PB1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0016586cellular_componentRSC-type complex
B0006338biological_processchromatin remodeling
B0016586cellular_componentRSC-type complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI A 1
ChainResidue
AHOH62
AHOH63
AHOH64
AHOH68
AHIS567
BGLU588

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 3
ChainResidue
AHIS541
ALYS547

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A 4
ChainResidue
ALYS584
BPRO597
AHIS580

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NI B 2
ChainResidue
BHOH60
BHOH61
BHOH67
BGLU532
BHIS580
BLYS584

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues53
DetailsBROMODOMAIN_1 Bromodomain signature. VkpSkkdyP.......DYYkiIlepMdlkiIehnirndk..Yageegmiedmkl.MfrNArhY
ChainResidueDetails
AVAL516-TYR568

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER466
BSER466

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER477
BSER477

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER604
BSER604

site_idSWS_FT_FI4
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS479
ALYS559
BLYS479
BLYS559

223166

PDB entries from 2024-07-31

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