6P6G

Co-crystal Structure of human SMYD3 with Isoxazole Amides Inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
A	0000993	molecular_function	RNA polymerase II complex binding
A	0001162	molecular_function	RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006334	biological_process	nucleosome assembly
A	0008168	molecular_function	methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0014904	biological_process	myotube cell development
A	0016740	molecular_function	transferase activity
A	0032259	biological_process	methylation
A	0042054	molecular_function	histone methyltransferase activity
A	0045184	biological_process	establishment of protein localization
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	0140939	molecular_function	histone H4 methyltransferase activity
A	0140954	molecular_function	histone H3K36 dimethyltransferase activity
A	0140999	molecular_function	histone H3K4 trimethyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 501

Chain	Residue
A	CYS208
A	CYS261
A	CYS263
A	CYS266

---

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 502

Chain	Residue
A	CYS62
A	CYS65
A	HIS83
A	CYS87

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 503

Chain	Residue
A	CYS52
A	CYS71
A	CYS75
A	CYS49

---

site_id	AC4
Number of Residues	6
Details	binding site for residue MG A 504

Chain	Residue
A	HOH696
A	HOH741
A	HOH786
A	HOH811
A	HOH966
A	HOH969

---

site_id	AC5
Number of Residues	6
Details	binding site for residue MG A 505

Chain	Residue
A	HOH632
A	HOH643
A	HOH653
A	HOH670
A	HOH681
A	HOH871

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL A 506

Chain	Residue
A	ASP332
A	ASP336
A	GLN372
A	LYS375
A	HOH684
A	HOH808
A	HOH823

---

site_id	AC7
Number of Residues	9
Details	binding site for residue GOL A 507

Chain	Residue
A	SER213
A	ILE214
A	CYS238
A	HIS366
A	PRO367
A	LUP510
A	HOH648
A	HOH691
A	HOH701

---

site_id	AC8
Number of Residues	6
Details	binding site for residue GOL A 508

Chain	Residue
A	PRO99
A	MET113
A	GLY115
A	GLN146
A	THR150
A	HOH715

---

site_id	AC9
Number of Residues	21
Details	binding site for residue SAH A 509

Chain	Residue
A	ARG14
A	ASN16
A	TYR124
A	GLU130
A	ASN132
A	CYS180
A	ASN181
A	SER202
A	LEU204
A	ASN205
A	HIS206
A	TYR239
A	TYR257
A	PHE259
A	HOH639
A	HOH647
A	HOH680
A	HOH719
A	HOH771
A	HOH774
A	HOH793

---

site_id	AD1
Number of Residues	20
Details	binding site for residue LUP A 510

Chain	Residue
A	CYS180
A	ASN181
A	SER182
A	PHE183
A	THR184
A	CYS186
A	GLU192
A	ILE237
A	TYR239
A	ASP241
A	TYR257
A	LEU290
A	GLU294
A	LYS329
A	CYS333
A	VAL368
A	GOL507
A	HOH602
A	HOH759
A	HOH810

---

Functional Information from PROSITE/UniProt

site_id	PS01360
Number of Residues	39
Details	ZF_MYND_1 Zinc finger MYND-type signature. Cdr..Cllgkeklmr........CsqCrvakYCsakCqkkawpd..Hkre.C

Chain	Residue	Details
A	CYS49-CYS87

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	236
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	38
Details	Zinc finger: {"description":"MYND-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	156
Details	Region: {"description":"C-terminal domain; essential for histone methyltransferase activity, nuclear localization and mediates interaction with HSP90AA1","evidences":[{"source":"PubMed","id":"25738358","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---