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1OYX

CRYSTAL STRUCTURE OF 3-MBT REPEATS OF LETHAL (3) MALIGNANT BRAIN TUMOR (SELENO-MET) AT 1.85 ANGSTROM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0006355biological_processregulation of DNA-templated transcription
B0005634cellular_componentnucleus
B0006355biological_processregulation of DNA-templated transcription
C0005634cellular_componentnucleus
C0006355biological_processregulation of DNA-templated transcription
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
BTYR275
BSER276
BHIS279
BLYS307

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 2002
ChainResidue
APRO446
CTYR275
CSER276
CHIS279
CLYS307

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 2003
ChainResidue
CARG356
CTRP389
CCYS390
CSER394
CTYR396
CARG444
CASP495

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2004
ChainResidue
BHIS482
BASP484
BGLY485

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 2005
ChainResidue
AHIS482
AGLY485

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 C 2006
ChainResidue
CLYS235
CSER315
CTRP316
CSER317

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 2007
ChainResidue
CLYS298
CLYS330
CHIS338

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2008
ChainResidue
ALYS235
AGLU297
ASER315
ATRP316
ASER317

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2009
ChainResidue
ALYS442
BSER487
BHIS488

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 2010
ChainResidue
APRO329
ALYS330
AHIS331

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2011
ChainResidue
BARG460
BHIS498
BHOH2027
BHOH2106
BHOH2152

site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 2012
ChainResidue
AARG460
AHIS498

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2013
ChainResidue
ATYR490
AHOH2097
BPRO221
BVAL222
BHOH2210

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2014
ChainResidue
BLYS235
BSER315
BTRP316
BSER317
BHOH2142

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 1011
ChainResidue
APHE256
APHE272
ATYR275
ASER276
AHIS279
ALYS307

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 1012
ChainResidue
AASP355
AASN358
ACYS363
APHE379
ATRP382
ATYR386

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MES B 1021
ChainResidue
BPHE256
BPHE272
BHIS279

site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES B 1022
ChainResidue
BASP355
BASN358
BCYS363
BPHE379
BTRP382
BTYR386
CHOH2180

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MES B 1023
ChainResidue
BASP459
BARG461
BPHE483
BTRP486

site_idCC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MES C 1031
ChainResidue
CPHE256
CTYR275
CHIS279

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES C 1032
ChainResidue
CASP355
CASN358
CPHE379
CTRP382
CTYR386

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Mediates recognition of monomethylated and dimethylated peptides
ChainResidueDetails
ACYS423
BCYS423
CCYS423

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Positioned at the entrance of MBT 2 and is required for recognition of monomethylated and dimethylated peptides
ChainResidueDetails
ALYS426
BLYS426
CLYS426

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PDB entries from 2024-04-17

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