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3OOI

Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0042054molecular_functionhistone methyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 232
ChainResidue
ACYS172
ACYS219
ACYS221
ACYS226

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 233
ChainResidue
ACYS44
ACYS46
ACYS54
ACYS60

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 234
ChainResidue
ACYS69
ACYS74
ACYS80
ACYS54

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 235
ChainResidue
AGLY77
AGLY78
ATHR98
ALEU99
AGLN100
AARG101
AHOH322
AHOH383
AHOH585
AHOH607

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 236
ChainResidue
AILE22
ALYS23
AVAL24
AARG26
AHOH414

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE SAM A 237
ChainResidue
AARG101
ATRP103
ATHR143
AASN144
APHE145
ATYR146
AARG166
AASN169
AHIS170
ATYR207
AASN214
AVAL218
ACYS219
ALYS220
ALEU230
AHOH277
AHOH278
AHOH366
AHOH401
AHOH458

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AARG101
ATHR143
AASN169

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:21196496
ChainResidueDetails
AASN214
ALYS220

221716

PDB entries from 2024-06-26

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