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6J2P

Crystal structure of Saccharomyces cerevisiae Spp1 in complex with H3K4me3

Functional Information from GO Data
ChainGOidnamespacecontents
A0048188cellular_componentSet1C/COMPASS complex
B0048188cellular_componentSet1C/COMPASS complex
C0048188cellular_componentSet1C/COMPASS complex
D0048188cellular_componentSet1C/COMPASS complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 201
ChainResidue
ACYS39
ACYS42
ACYS66
ACYS69

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 202
ChainResidue
ACYS93
ACYS98
ACYS109
AHIS113

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 203
ChainResidue
ACYS27
AHIS47
ACYS50
ACYS25

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 201
ChainResidue
BCYS25
BCYS27
BHIS47
BCYS50

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 202
ChainResidue
BCYS39
BCYS42
BCYS66
BCYS69

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 203
ChainResidue
BCYS93
BCYS98
BCYS109
BHIS113

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN C 201
ChainResidue
CCYS25
CCYS27
CHIS47
CCYS50

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN C 202
ChainResidue
CCYS39
CCYS42
CCYS66
CCYS69
CTHR74

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN C 203
ChainResidue
CCYS93
CCYS98
CCYS109
CHIS113

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN D 201
ChainResidue
DCYS25
DCYS27
DHIS47
DCYS50

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN D 202
ChainResidue
DCYS39
DCYS42
DCYS66
DCYS69

site_idAD3
Number of Residues3
Detailsbinding site for residue ZN D 203
ChainResidue
DCYS93
DCYS98
DCYS109

Functional Information from PROSITE/UniProt
site_idPS01359
Number of Residues45
DetailsZF_PHD_1 Zinc finger PHD-type signature. Ci.Ckrpdygelm....................................VgCdg..Cddw.FHftClhipeqfkdlvfs................................FyCpyC
ChainResidueDetails
ACYS25-CYS69

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708
ChainResidueDetails
EM3L4
FM3L4
GM3L4
HM3L4

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00146, ECO:0000269|PubMed:31253666, ECO:0007744|PDB:6J2P
ChainResidueDetails
ACYS25
BCYS27
BCYS39
BCYS42
BHIS47
BCYS50
BCYS66
BCYS69
CCYS25
CCYS27
CCYS39
ACYS27
CCYS42
CHIS47
CCYS50
CCYS66
CCYS69
DCYS25
DCYS27
DCYS39
DCYS42
DHIS47
ACYS39
DCYS50
DCYS66
DCYS69
ACYS42
AHIS47
ACYS50
ACYS66
ACYS69
BCYS25

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:31253666, ECO:0007744|PDB:6J2P
ChainResidueDetails
AASP97
CCYS102
CHIS113
CPHE117
DASP97
DCYS102
DHIS113
DPHE117
ACYS102
AHIS113
APHE117
BASP97
BCYS102
BHIS113
BPHE117
CASP97

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR87
BTHR87
CTHR87
DTHR87

227111

PDB entries from 2024-11-06

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