Structure of PDB 5dxj Chain D

Receptor sequence
>5dxjD (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB5dxj Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.
ChainD
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D165 E257 E266 H414
Catalytic site (residue number reindexed from 1) D32 E124 E133 H281
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 SFG D Y149 F150 Y153 Q159 M162 R168 G192 C193 G194 I197 L198 E214 A215 K241 V242 E243 E257 M268 Y16 F17 Y20 Q26 M29 R35 G59 C60 G61 I64 L65 E81 A82 K108 V109 E110 E124 M135
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:5dxj, PDBe:5dxj, PDBj:5dxj
PDBsum5dxj
PubMed26551522
UniProtQ86X55|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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