Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3BO5

Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0008270molecular_functionzinc ion binding
A0042054molecular_functionhistone methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS61
ACYS75
ACYS104
ACYS108

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 302
ChainResidue
ACYS68
ACYS104
ACYS110
ACYS114

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
ACYS63
ACYS68
ACYS73
ACYS61

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 304
ChainResidue
ACYS212
ACYS273
ACYS275
ACYS280

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 305
ChainResidue
ALYS135
AGLY136
ATRP137
AASN177
ATYR178
AARG206
AASN209
AHIS210
ATYR248
AARG263
APRO272
ACYS273
ATYR274
ACYS275
ALEU284
APHE286
AHOH427
AHOH473
AHOH515
AHOH524
AHOH627

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
ACYS63
AVAL64
ALYS65
ATHR66

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AASN22
ALYS121
AGLN124
AHOH642

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING:
ChainResidueDetails
ASER74
AGLY148
AVAL191
AARG222
ASER225
APHE286
ASER288
ALEU76
AASN81
ASER86
ALEU88
AARG117
ALYS121
ALEU123
APHE127

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190
ChainResidueDetails
AILE219

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon