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1ZR3

Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B)

Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MES A 500
ChainResidue
APRO215
AASN316
AHOH502
AHOH512
AHOH583
ATHR216
AASN217
ATYR221
AGLY223
ASER275
AGLY312
AGLY314
AARG315

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0D2UG83
ChainResidueDetails
AASP203
BILE204
BVAL226
BSER275
BGLY312
BSER313
BGLY314
BASN316
CASP203
CILE204
CVAL226
AILE204
CSER275
CGLY312
CSER313
CGLY314
CASN316
DASP203
DILE204
DVAL226
DSER275
DGLY312
AVAL226
DSER313
DGLY314
DASN316
ASER275
AGLY312
ASER313
AGLY314
AASN316
BASP203

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER170
BSER170
CSER170
DSER170

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER173
BSER173
CSER173
DSER173

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR178
BTHR178
CTHR178
DTHR178

site_idSWS_FT_FI5
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS167
CLYS189
CLYS320
DLYS167
DLYS189
DLYS320
ALYS189
ALYS320
BLYS167
BLYS189
BLYS320
CLYS167

218853

PDB entries from 2024-04-24

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