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6Z2A

Structure of Clr4 mutant - F256A/F310A/F427A bound to SAH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0008270molecular_functionzinc ion binding
A0042054molecular_functionhistone methyltransferase activity
A0046974molecular_functionhistone H3K9 methyltransferase activity
B0005634cellular_componentnucleus
B0008270molecular_functionzinc ion binding
B0042054molecular_functionhistone methyltransferase activity
B0046974molecular_functionhistone H3K9 methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS260
ACYS262
ACYS268
ACYS276

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
ACYS260
ACYS278
ACYS307
ACYS311

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
ACYS307
ACYS313
ACYS317
ACYS268

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 504
ChainResidue
ACYS412
ACYS477
ACYS479
ACYS484

site_idAC5
Number of Residues18
Detailsbinding site for residue SAH A 505
ChainResidue
ALYS338
AGLY339
ATRP340
AGLY378
AILE379
ATYR381
AARG406
APHE407
APHE408
AASN409
AHIS410
ATYR451
ALYS455
AARG475
ACYS477
ALYS478
APHE489
AHOH612

site_idAC6
Number of Residues2
Detailsbinding site for residue MG A 506
ChainResidue
AASP386
AGLY453

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 501
ChainResidue
BCYS260
BCYS262
BCYS268
BCYS276

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 502
ChainResidue
BCYS268
BCYS307
BCYS313
BCYS317

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 503
ChainResidue
BCYS260
BCYS278
BCYS307
BCYS311

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 504
ChainResidue
BCYS412
BCYS477
BCYS479
BCYS484

site_idAD2
Number of Residues15
Detailsbinding site for residue SAH B 505
ChainResidue
BLYS338
BGLY339
BTRP340
BGLY378
BILE379
BTYR381
BARG406
BPHE408
BASN409
BHIS410
BTYR451
BARG475
BGLN476
BCYS477
BLYS478

site_idAD3
Number of Residues4
Detailsbinding site for residue MG B 506
ChainResidue
AASP291
AGLN293
BARG244
BGLU360

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:12389037, ECO:0000269|PubMed:30051891
ChainResidueDetails
BCYS260
BCYS262
BCYS268
BCYS276
BCYS278
BCYS307
BCYS311
BCYS313
BCYS317

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:30051891
ChainResidueDetails
BLYS338
BPHE407
BCYS412
BCYS477
BCYS479
BCYS484

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190
ChainResidueDetails
BTYR381
BARG406

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-methyllysine; by autocatalysis; alternate => ECO:0000269|PubMed:30051891
ChainResidueDetails
BLYS455

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0000269|PubMed:30051891
ChainResidueDetails
BLYS464

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PDB entries from 2024-08-07

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