Structure of PDB 5u4x Chain C

Receptor sequence
>5u4xC (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
AVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFKDKIVLDVGCGS
GILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDRIVVIPGKVEEV
SLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGNMFPTIGDVHLA
PFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEYFRQPVVDTFDI
RILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLVHGLAFWFDVAF
IGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTLSGTCLLIANKR
QSYDISIVAQVDQTGSKSSNLLDLKNPFFR
3D structure
PDB5u4x TP-064, a potent and selective small molecule inhibitor of PRMT4 for multiple myeloma.
ChainC
Resolution1.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D166 E258 E267 H415
Catalytic site (residue number reindexed from 1) D20 E112 E121 H269
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SAH C Y150 F151 Y154 Q160 M163 R169 G193 C194 I198 L199 E215 A216 K242 V243 M269 S272 Y4 F5 Y8 Q14 M17 R23 G47 C48 I52 L53 E69 A70 K96 V97 M123 S126 BindingDB: Ki=400nM
BS02 7VM C Y150 F153 Y154 M163 E258 M260 Y262 N266 E267 H415 Q447 K471 P473 F475 Y4 F7 Y8 M17 E112 M114 Y116 N120 E121 H269 Q301 K325 P327 F329
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5u4x, PDBe:5u4x, PDBj:5u4x
PDBsum5u4x
PubMed29719619
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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