5VCY

CRYSTAL STRUCTURE OF HUMAN MYT1 KINASE DOMAIN IN COMPLEX WITH BOSUTINIB

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue DB8 A 401

Chain	Residue
A	LEU116
A	CYS190
A	GLY191
A	GLN196
A	ASN238
A	PHE240
A	DMS406
A	HOH617
A	HOH619
A	ALA137
A	VAL138
A	LYS139
A	GLU157
A	VAL171
A	LEU185
A	THR187
A	GLU188

---

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 402

Chain	Residue
A	GLU310
A	GLN314
A	GLU331
A	HOH584

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 403

Chain	Residue
A	PRO148
A	PHE324
A	EDO404
A	HOH670

---

site_id	AC4
Number of Residues	4
Details	binding site for residue EDO A 404

Chain	Residue
A	PHE145
A	GLY181
A	EDO403
A	HOH652

---

site_id	AC5
Number of Residues	4
Details	binding site for residue PEG A 405

Chain	Residue
A	SER114
A	ARG115
A	GLN313
A	HOH564

---

site_id	AC6
Number of Residues	4
Details	binding site for residue DMS A 406

Chain	Residue
A	LYS139
A	ASP251
A	DB8401
A	HOH501

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGHGSYGEVFkVrskedgrl..........YAVK

Chain	Residue	Details
A	LEU116-LYS139

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHlDVKpaNIFL

Chain	Residue	Details
A	LEU229-LEU241

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP233

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU116
A	LYS139

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P30291

Chain	Residue	Details
A	ASN238
A	ASP251
A	GLY253

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER94

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER120

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER143

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	SER160

---