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3B3J

The 2.55 A crystal structure of the apo catalytic domain of coactivator-associated arginine methyl transferase I(CARM1:28-507, residues 28-146 and 479-507 not ordered)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0018216biological_processpeptidyl-arginine methylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEN A 1001
ChainResidue
AGLU334
AARG337
AASP450
ALEU467
AASP469

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN A 2001
ChainResidue
APHE475
AHOH6030
APHE153
ATYR156
ALEU157
AGLN165

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEN A 3001
ChainResidue
AHIS275
AGLU365
AILE442
AASP450
ASER452

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BEN A 4001
ChainResidue
APHE153
ATYR154
ATRP416
ATYR417
AGLN418
AHOH6009
AHOH6030

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BEN A 5001
ChainResidue
ALYS277
ALYS281
ALEU361
AGLU362

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BEN A 6001
ChainResidue
ALEU264
ALEU270
AGLY291
AASP292
APHE360
AILE371

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:17882262
ChainResidueDetails
AGLN160
AARG169
AGLY193
AGLU215
AGLU244
ASER272

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q86X55
ChainResidueDetails
ASER217

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86X55
ChainResidueDetails
ALYS228

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
AGLU258
AGLU267

222415

PDB entries from 2024-07-10

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