Structure of PDB 3sr4 Chain A

Receptor sequence
>3sr4A (length=328) Species: 9606 (Homo sapiens) [Search protein sequence]
LELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLA
MENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPST
GLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMT
DDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRK
WMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLK
ERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVS
WTGKPVSYYLHTIDRTILENYFSSLKNP
3D structure
PDB3sr4 Selective Inhibitors of Histone Methyltransferase DOT1L: Design, Synthesis, and Crystallographic Studies.
ChainA
Resolution2.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.1.1.360: [histone H3]-lysine(79) N-trimethyltransferase.
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 TT8 A G137 E138 T139 D161 G163 S164 Q168 V169 E186 K187 G221 D222 F223 F245 G133 E134 T135 D157 G159 S160 Q164 V165 E182 K183 G217 D218 F219 F241 MOAD: Ki=0.29uM
PDBbind-CN: -logKd/Ki=6.54,Ki=0.29uM
BindingDB: Ki=290nM
Gene Ontology
Molecular Function
GO:0031151 histone H3K79 methyltransferase activity
Biological Process
GO:0051726 regulation of cell cycle

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3sr4, PDBe:3sr4, PDBj:3sr4
PDBsum3sr4
PubMed21936531
UniProtQ8TEK3|DOT1L_HUMAN Histone-lysine N-methyltransferase, H3 lysine-79 specific (Gene Name=DOT1L)

[Back to BioLiP]