Structure of PDB 4h12 Chain A

Receptor sequence

>4h12A (length=233) Species: 9606 (Homo sapiens)

PSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTEMQCECTPLSKDE
RAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTE
KKGWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMA
LKNDEIIDATQKGNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPS
GSELTFDYQFQRYGKEAQKCFCGSANCRGYLGG

3D structure

• PDB: 4h12 Sinefungin Derivatives as Inhibitors and Structure Probes of Protein Lysine Methyltransferase SETD2.
• Chain: A
• Resolution: 2.06 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y1579 Y1666
• Catalytic site (residue number reindexed from 1): Y121 Y208
• Enzyme Commision number: 2.1.1.-
  2.1.1.359: [histone H3]-lysine(36) 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	ZN	A	C1499 C1501 C1516 C1520	C41 C43 C58 C62
BS02	ZN	A	C1516 C1529 C1533 C1539	C58 C71 C75 C81
BS03	ZN	A	C1631 C1678 C1680 C1685	C173 C220 C222 C227
BS04	SAH	A	K1560 G1561 W1562 H1603 Y1604 Y1605 R1625 F1626 N1628 H1629 Y1666 R1670 Q1676 C1678 F1679 L1689	K102 G103 W104 H145 Y146 Y147 R167 F168 N170 H171 Y208 R212 Q218 C220 F221 L231

Gene Ontology

Molecular Function

• GO:0016279 protein-lysine N-methyltransferase activity
• GO:0042054 histone methyltransferase activity
• GO:0046975 histone H3K36 methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:4h12, PDBe:4h12, PDBj:4h12
• PDBsum: 4h12
• PubMed: 23043551
• UniProt: Q9BYW2|SETD2_HUMAN Histone-lysine N-methyltransferase SETD2 (Gene Name=SETD2)