Structure of PDB 1h3i Chain B

Receptor sequence
>1h3iB (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
FFFDGSTLEGYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTD
GRLIFKGQYKDNIRHGVCWIYYPDGGSLVGEVNEDGEMTGEKIAYVYPDE
RTALYGKFIDGEMIEGKLATLMSTEEGRPHFELMPGNSVYHFDKSTSSCI
STNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNTVMSFYNGVRIT
HQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFTP
NCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGK
3D structure
PDB1h3i Crystal Structure and Functional Analysis of the Histone Methyltransferase Set7/9
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) Y245 H293 H297 Y305 Y335
Catalytic site (residue number reindexed from 1) Y194 H242 H246 Y254 Y284
Enzyme Commision number 2.1.1.364: [histone H3]-lysine(4) N-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 MG B E279 H283 E228 H232
Gene Ontology
Molecular Function
GO:0016279 protein-lysine N-methyltransferase activity
GO:0140945 histone H3K4 monomethyltransferase activity
Biological Process
GO:0006355 regulation of DNA-templated transcription
Cellular Component
GO:0005694 chromosome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1h3i, PDBe:1h3i, PDBj:1h3i
PDBsum1h3i
PubMed12372304
UniProtQ8WTS6|SETD7_HUMAN Histone-lysine N-methyltransferase SETD7 (Gene Name=SETD7)

[Back to BioLiP]