Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3RC0

Human SETD6 in complex with RelA Lys310 peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005829cellular_componentcytosol
A0008168molecular_functionmethyltransferase activity
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0016740molecular_functiontransferase activity
A0018022biological_processpeptidyl-lysine methylation
A0018026biological_processpeptidyl-lysine monomethylation
A0019827biological_processstem cell population maintenance
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0032259biological_processmethylation
A0048863biological_processstem cell differentiation
A0050727biological_processregulation of inflammatory response
A0051059molecular_functionNF-kappaB binding
A1904047molecular_functionS-adenosyl-L-methionine binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0008168molecular_functionmethyltransferase activity
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0016740molecular_functiontransferase activity
B0018022biological_processpeptidyl-lysine methylation
B0018026biological_processpeptidyl-lysine monomethylation
B0019827biological_processstem cell population maintenance
B0032088biological_processnegative regulation of NF-kappaB transcription factor activity
B0032259biological_processmethylation
B0048863biological_processstem cell differentiation
B0050727biological_processregulation of inflammatory response
B0051059molecular_functionNF-kappaB binding
B1904047molecular_functionS-adenosyl-L-methionine binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 474
ChainResidue
ALEU150
AGLY151
AARG152
ALEU153
APHE158
AGLN215

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 475
ChainResidue
AGLU187
ASER120
ATRP122
AASN183

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 476
ChainResidue
AARG31
ALEU424
ATYR427
AALA428
AHOH521

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 477
ChainResidue
AGLU396
AGLU397
AGLY398
ASER399
BPRO136

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 478
ChainResidue
AVAL300
ATYR444
ATRP449
AGLN452
AHOH590
BLYS441

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 479
ChainResidue
AARG30
ALEU34
ALEU36
AHOH651

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 480
ChainResidue
AHOH49
ALEU253
AVAL300
ASAM484
AHOH590
AHOH595
BLYS441

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 481
ChainResidue
AASN440
AGLU442
BGLY74
BEDO477

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 482
ChainResidue
ALEU362
AGLU364
AGLU365
AGLU366
AHOH628
AHOH701

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 483
ChainResidue
AGLN324
AASN418
ALEU422
AGLN425
AHOH563
AHOH576

site_idBC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAM A 484
ChainResidue
AVAL72
AALA73
AGLY74
ATYR75
AALA222
ATYR223
AASP248
AILE249
ALEU250
AASN251
AHIS252
ATYR285
ATYR297
APHE299
AEDO480
AHOH523
AHOH551
AHOH560
AHOH578
AHOH596
AHOH619

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 474
ChainResidue
BVAL300
BTYR444
BTRP449
BGLN452
BHOH562
BHOH603

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 475
ChainResidue
BGLY170
BTHR171
BGLY172
BGLU175
BGLN314

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 476
ChainResidue
AGLU197
AARG208
BASN255
BHOH649

site_idBC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO B 477
ChainResidue
AASN440
ALYS441
AGLU442
AEDO481
BVAL72
BALA73
BTRP449
BSAM480
BHOH528
BHOH582

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 478
ChainResidue
BSER120
BASN183
BGLU187

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 479
ChainResidue
BGLU154
BTRP159
BTRP449
BARG450
BGLN453
BHOH496

site_idBC9
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAM B 480
ChainResidue
BVAL72
BALA73
BGLY74
BTYR75
BALA222
BTYR223
BASP248
BILE249
BLEU250
BASN251
BHIS252
BTYR285
BTYR297
BPHE299
BEDO477
BHOH545
BHOH547
BHOH574
BHOH593
BHOH600
BHOH608

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-methyllysine; by SETD6; alternate => ECO:0000250|UniProtKB:Q04207
ChainResidueDetails
PLYS310
BLEU146
BALA247
BASP248
BLEU250
BILE275
BGLY286
BALA321
QLYS310
AALA247
AASP248
ALEU250
AILE275
AGLY286
AALA321
BLEU97

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC/PRKCZ => ECO:0000250|UniProtKB:Q04207
ChainResidueDetails
PSER311
QSER311
BLYS39
BPHE203

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-methylated lysine; by autocatalysis => ECO:0000305|PubMed:30189201
ChainResidueDetails
AGLU396
BGLU396

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon