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4GY5

Crystal structure of the tandem tudor domain and plant homeodomain of UHRF1 with Histone H3K9me3

Functional Information from GO Data
ChainGOidnamespacecontents
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0030527molecular_functionstructural constituent of chromatin
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0030527molecular_functionstructural constituent of chromatin
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS302
ACYS305
ACYS313
ACYS316

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 402
ChainResidue
ACYS318
ACYS321
AHIS341
ACYS344

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 403
ChainResidue
ACYS336
ACYS360
ACYS363
ACYS333

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS333
BCYS336
BCYS360
BCYS363

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS302
BCYS305
BCYS313
BCYS316

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 403
ChainResidue
BCYS318
BCYS321
BHIS341
BCYS344

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN C 401
ChainResidue
CCYS302

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues62
DetailsZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC
ChainResidueDetails
ACYS302-CYS363

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:16567635
ChainResidueDetails
EARG2
FARG2
CASN310-ASP366
DASN310-ASP366

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
ChainResidueDetails
ETHR3
FTHR3
CCYS316
DCYS316

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
ChainResidueDetails
ELYS4
FLYS4
BPRO327
BGLN330
CPRO327
CGLN330
DPRO327
DGLN330

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
ChainResidueDetails
EGLN5
FGLN5
CSER165
DSER165

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
ChainResidueDetails
ETHR6
FTHR6
CSER287
DSER287

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P84244
ChainResidueDetails
EARG8
FARG8
CSER298
DSER298

site_idSWS_FT_FI7
Number of Residues2
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, ECO:0000269|PubMed:7309716
ChainResidueDetails
EM3L9
FM3L9
BLYS279
CLYS279
DLYS279

site_idSWS_FT_FI8
Number of Residues2
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:15851689, ECO:0000269|PubMed:16185088
ChainResidueDetails
ESER10
FSER10

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803
ChainResidueDetails
ETHR11
FTHR11

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ELYS14
FLYS14

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635
ChainResidueDetails
EARG17
FARG17

219140

PDB entries from 2024-05-01

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