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3U88

Crystal structure of human menin in complex with MLL1 and LEDGF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000165biological_processMAPK cascade
A0000400molecular_functionfour-way junction DNA binding
A0000403molecular_functionY-form DNA binding
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0000976molecular_functiontranscription cis-regulatory region binding
A0001933biological_processnegative regulation of protein phosphorylation
A0002076biological_processosteoblast development
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003690molecular_functiondouble-stranded DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005788cellular_componentendoplasmic reticulum lumen
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006325biological_processchromatin organization
A0006357biological_processregulation of transcription by RNA polymerase II
A0006974biological_processDNA damage response
A0008285biological_processnegative regulation of cell population proliferation
A0009411biological_processresponse to UV
A0010332biological_processresponse to gamma radiation
A0016363cellular_componentnuclear matrix
A0017053cellular_componenttranscription repressor complex
A0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
A0030674molecular_functionprotein-macromolecule adaptor activity
A0032154cellular_componentcleavage furrow
A0032991cellular_componentprotein-containing complex
A0035097cellular_componenthistone methyltransferase complex
A0043433biological_processnegative regulation of DNA-binding transcription factor activity
A0044665cellular_componentMLL1/2 complex
A0045064biological_processT-helper 2 cell differentiation
A0045668biological_processnegative regulation of osteoblast differentiation
A0045736biological_processnegative regulation of cyclin-dependent protein serine/threonine kinase activity
A0045786biological_processnegative regulation of cell cycle
A0045815biological_processtranscription initiation-coupled chromatin remodeling
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046329biological_processnegative regulation of JNK cascade
A0051219molecular_functionphosphoprotein binding
A0051974biological_processnegative regulation of telomerase activity
A0070412molecular_functionR-SMAD binding
A0071339cellular_componentMLL1 complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000165biological_processMAPK cascade
B0000400molecular_functionfour-way junction DNA binding
B0000403molecular_functionY-form DNA binding
B0000781cellular_componentchromosome, telomeric region
B0000785cellular_componentchromatin
B0000976molecular_functiontranscription cis-regulatory region binding
B0001933biological_processnegative regulation of protein phosphorylation
B0002076biological_processosteoblast development
B0003677molecular_functionDNA binding
B0003682molecular_functionchromatin binding
B0003690molecular_functiondouble-stranded DNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005788cellular_componentendoplasmic reticulum lumen
B0005829cellular_componentcytosol
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006357biological_processregulation of transcription by RNA polymerase II
B0006974biological_processDNA damage response
B0008285biological_processnegative regulation of cell population proliferation
B0009411biological_processresponse to UV
B0010332biological_processresponse to gamma radiation
B0016363cellular_componentnuclear matrix
B0017053cellular_componenttranscription repressor complex
B0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
B0030674molecular_functionprotein-macromolecule adaptor activity
B0032154cellular_componentcleavage furrow
B0032991cellular_componentprotein-containing complex
B0035097cellular_componenthistone methyltransferase complex
B0043433biological_processnegative regulation of DNA-binding transcription factor activity
B0044665cellular_componentMLL1/2 complex
B0045064biological_processT-helper 2 cell differentiation
B0045668biological_processnegative regulation of osteoblast differentiation
B0045736biological_processnegative regulation of cyclin-dependent protein serine/threonine kinase activity
B0045786biological_processnegative regulation of cell cycle
B0045815biological_processtranscription initiation-coupled chromatin remodeling
B0045892biological_processnegative regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046329biological_processnegative regulation of JNK cascade
B0051219molecular_functionphosphoprotein binding
B0051974biological_processnegative regulation of telomerase activity
B0070412molecular_functionR-SMAD binding
B0071339cellular_componentMLL1 complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD A 611
ChainResidue
ASER132
ATYR133
APHE134
ALYS135
BCHD611

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CHD B 611
ChainResidue
BLYS135
ACHD611
BSER132
BTYR133
BPHE134

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 0BR B 612
ChainResidue
A0BR612
BTRP126
BSER130
BARG131
BTRP198
BASN203

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GGB A 613
ChainResidue
ATYR133
APHE134
AARG137
ALYS151

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 0BR A 612
ChainResidue
ATRP126
ALEU129
ASER130
AARG131
ATRP198
AASN203
B0BR612

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GGB B 615
ChainResidue
BTYR133
BPHE134
BARG137
BLYS151

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GGB A 614
ChainResidue
AARG108
AGLY111
AVAL112
ASER113
AARG171

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLV A 615
ChainResidue
ALYS135
AASP136
ASER154
ATRP198
AGLY200

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLV A 616
ChainResidue
AGLU195
ATHR197
AARG206
ATYR222

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GLV A 617
ChainResidue
AGLU408
AALA411
AHIS412
AARG415
ALEU551

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GLV B 616
ChainResidue
BLYS135
BASP136
BSER154
BTRP198
BGLY200
BLYS201

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 N 1
ChainResidue
BARG330
NGLY23
NARG24
NARG25
NGLY26

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 M 2
ChainResidue
MGLY14
MTHR15
MGLY23
MARG24
MARG25
MGLY26

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 618
ChainResidue
ATHR56
ALYS377
AARG446

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 619
ChainResidue
AARG275
BLYS310

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 617
ChainResidue
BARG108
BGLY111
BGLY169
BARG171

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GGB C 108
ChainResidue
CGGB109
CARG405

site_idBC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 618
ChainResidue
BLYS377
BARG446

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GGB C 109
ChainResidue
CGGB108
CLEU363
CLYS364
CILE365

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GLV C 113
ChainResidue
AARG98
CARG404
CTHR417
CASN421

site_idCC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GLV D 114
ChainResidue
DTHR417
DASN421

site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 N 154
ChainResidue
BGLY2
DLYS424
NARG130

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 M 154
ChainResidue
AGLY2
CLYS424
MARG130
MGLY134
MGLU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER434
DSER434
NSER136
NSER142

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:29997176, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
MSER153
NSER153

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR594
BTHR594

219869

PDB entries from 2024-05-15

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