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2FSA

Crystal structure of PHD finger-linker-bromodomain fragment of human BPTF in the H3(1-15)K4ME2 bound state

Functional Information from GO Data
ChainGOidnamespacecontents
A0006357biological_processregulation of transcription by RNA polymerase II
A0016589cellular_componentNURF complex
B0006357biological_processregulation of transcription by RNA polymerase II
B0016589cellular_componentNURF complex
C0006357biological_processregulation of transcription by RNA polymerase II
C0016589cellular_componentNURF complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS11
ACYS13
AHIS34
ACYS37

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS26
ACYS29
ACYS53
ACYS56

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BCYS13
BHIS34
BCYS37
BCYS11

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BCYS26
BCYS29
BCYS53
BCYS56

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 505
ChainResidue
CCYS11
CCYS13
CHIS34
CCYS37

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 506
ChainResidue
CCYS26
CCYS29
CCYS53
CCYS56

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. AwpFlepvDpndap..DYYgvIkepMdlatMeervqrry..Yekltefvadmtk.IfdNCryY
ChainResidueDetails
AALA90-TYR147

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CiCktPYdeskfyigC
ChainResidueDetails
ACYS11-CYS26

site_idPS01359
Number of Residues46
DetailsZF_PHD_1 Zinc finger PHD-type signature. Ci.Cktpydeskfy...................................IgCdr..Cqnw.YHgrCvgilqseaelide................................YvCpqC
ChainResidueDetails
ACYS11-CYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
PARG2
BLYS8-THR59
CLYS8-THR59

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692
ChainResidueDetails
PTHR3
CTYR17
CTYR23
CTRP32
ATYR17
ATYR23
ATRP32
BTYR10
BTYR17
BTYR23
BTRP32
CTYR10

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
PMLY4

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
PGLN5

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
PTHR6

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
ChainResidueDetails
PARG8

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
PLYS9

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
ChainResidueDetails
PSER10

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
ChainResidueDetails
PTHR11

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
PLYS14

225946

PDB entries from 2024-10-09

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