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

5IS7

Crystal structure of mouse CARM1 in complex with decarboxylated SAH

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 Residues2
Detailsbinding site for residue PEG A 502
ChainResidue
APHE153
AGLU267

site_idAC2
Number of Residues1
Detailsbinding site for residue PEG A 503
ChainResidue
ATRP404

site_idAC3
Number of Residues15
Detailsbinding site for residue DSH A 504
ChainResidue
ALYS242
AVAL243
AGLU244
AGLU258
AMET260
AMET269
ASER272
AHIS415
ATRP416
ATYR150
ATYR154
AMET163
AGLY193
AGLU215
AALA216

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO B 501
ChainResidue
BTRP404

site_idAC5
Number of Residues1
Detailsbinding site for residue EDO B 502
ChainResidue
BGLU267

site_idAC6
Number of Residues17
Detailsbinding site for residue DSH B 503
ChainResidue
BTYR150
BPHE151
BTYR154
BMET163
BGLY193
BGLY195
BGLU215
BALA216
BLYS242
BVAL243
BGLU244
BGLU258
BMET260
BMET269
BSER272
BHIS415
BTRP416

site_idAC7
Number of Residues1
Detailsbinding site for residue EDO C 501
ChainResidue
CTRP404

site_idAC8
Number of Residues17
Detailsbinding site for residue DSH C 502
ChainResidue
CTYR150
CTYR154
CMET163
CGLY193
CGLY195
CGLU215
CALA216
CSER217
CLYS242
CVAL243
CGLU244
CGLU258
CMET260
CMET269
CSER272
CHIS415
CTRP416

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO D 501
ChainResidue
DASP393

site_idAD1
Number of Residues13
Detailsbinding site for residue DSH D 502
ChainResidue
DTYR150
DPHE151
DTYR154
DGLY193
DGLU215
DVAL243
DGLU244
DGLU258
DMET260
DGLU267
DMET269
DSER272
DHIS415

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

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon