Structure of PDB 5fub Chain A

Receptor sequence
>5fubA (length=337) Species: 7955 (Danio rerio) [Search protein sequence]
GDAWQDDEYFGNYGTLRLHLEMLSDKPRTETYRQVILSNSAALREKVVLD
LGCGTGVISLFCALLAKPAGVYAVEASSMAEHTEELVKQNGCDGVVTVFQ
ERAENLTLPTKVDVLVSEWMGNCLLFEYMLESVLLARDRWLKKGGMMWPS
SACLTIVPCQAFSDYRQKVEFWENPYGLNFSYLQSLAQKEFLSKPKFSHH
LQPEDCLSTPADVITLDMVTIQVSDLERLKGEFTFTVEKSGMFHGFTVWF
SAHFQCLEEDGPSIELNTGPYSEITHWKQTLFMLDAPVSVEEGDIIAGSI
RLQRNPIWRRHLSITFLWNINSTEVSTVKTKCFPMWR
3D structure
PDB5fub Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors.
ChainA
Resolution1.997 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D96 E189 E198 H347
Catalytic site (residue number reindexed from 1) D25 E118 E127 H276
Enzyme Commision number 2.1.1.125: Transferred entry: 2.1.1.319, 2.1.1.320, 2.1.1.321 and 2.1.1.322.
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 A Y80 F81 Y84 M93 R99 G123 C124 V128 E146 A147 R173 M200 S203 Y9 F10 Y13 M22 R28 G52 C53 V57 E75 A76 R102 M129 S132
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:5fub, PDBe:5fub, PDBj:5fub
PDBsum5fub
PubMed27879050
UniProtA1L1Q4

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