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5ISD

Crystal structure of mouse CARM1 in complex with inhibitor SA0592

Functional Information from GO Data
ChainGOidnamespacecontents
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0018216biological_processpeptidyl-arginine methylation
B0016274molecular_functionprotein-arginine N-methyltransferase activity
B0018216biological_processpeptidyl-arginine methylation
C0016274molecular_functionprotein-arginine N-methyltransferase activity
C0018216biological_processpeptidyl-arginine methylation
D0016274molecular_functionprotein-arginine N-methyltransferase activity
D0018216biological_processpeptidyl-arginine methylation
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue EDO A 501
ChainResidue
AM2M506

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 502
ChainResidue
ALEU280
ALYS281

site_idAC3
Number of Residues1
Detailsbinding site for residue PEG A 504
ChainResidue
AHOH608

site_idAC4
Number of Residues1
Detailsbinding site for residue PEG A 505
ChainResidue
AGLY284

site_idAC5
Number of Residues9
Detailsbinding site for residue M2M A 506
ChainResidue
ATYR262
AGLU267
AHIS415
ATRP416
AEDO501
ATYR154
AMET163
AGLU258
AMET260

site_idAC6
Number of Residues19
Detailsbinding site for residue SAO A 507
ChainResidue
ATYR150
APHE151
ATYR154
AGLN160
AMET163
AARG169
AGLY193
ACYS194
AGLY195
AILE198
AGLU215
AALA216
AGLY241
ALYS242
AVAL243
AGLU244
AMET269
ASER272
AHOH612

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO B 501
ChainResidue
BASP393
BTRP404

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO B 502
ChainResidue
BPHE153

site_idAC9
Number of Residues2
Detailsbinding site for residue PEG B 503
ChainResidue
BGLN251
BLYS278

site_idAD1
Number of Residues23
Detailsbinding site for residue 6CZ B 504
ChainResidue
BTYR150
BPHE151
BTYR154
BGLN160
BMET163
BARG169
BGLY193
BCYS194
BGLY195
BILE198
BGLU215
BALA216
BGLY241
BLYS242
BVAL243
BGLU244
BGLU258
BMET260
BGLU267
BMET269
BSER272
BHIS415
BTRP416

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO C 501
ChainResidue
CTYR150
CPHE153

site_idAD3
Number of Residues1
Detailsbinding site for residue EDO C 502
ChainResidue
CTRP404

site_idAD4
Number of Residues19
Detailsbinding site for residue SAO C 504
ChainResidue
CTYR150
CPHE151
CTYR154
CGLN160
CMET163
CARG169
CGLY193
CCYS194
CILE198
CGLU215
CALA216
CGLY241
CLYS242
CVAL243
CGLU244
CGLU258
CMET269
CSER272
CHOH609

site_idAD5
Number of Residues2
Detailsbinding site for residue EDO D 501
ChainResidue
DASP393
DTRP404

site_idAD6
Number of Residues18
Detailsbinding site for residue SAO D 502
ChainResidue
DGLU244
DMET269
DSER272
DHOH609
DTYR150
DPHE151
DTYR154
DGLN160
DMET163
DARG169
DGLY193
DCYS194
DGLY195
DILE198
DLEU199
DGLU215
DALA216
DVAL243

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:17882261
ChainResidueDetails
AGLN160
BGLU215
BGLU244
BSER272
CGLN160
CARG169
CGLY193
CGLU215
CGLU244
CSER272
DGLN160
AARG169
DARG169
DGLY193
DGLU215
DGLU244
DSER272
AGLY193
AGLU215
AGLU244
ASER272
BGLN160
BARG169
BGLY193

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19843527
ChainResidueDetails
ASER217
BSER217
CSER217
DSER217

site_idSWS_FT_FI3
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86X55
ChainResidueDetails
ALYS228
BLYS228
CLYS228
DLYS228

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PDB entries from 2024-07-10

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