5KGE

Crystal structure of PIM1 with inhibitor: 5-(3,4-dichlorophenyl)-1~{H}-pyrazol-3-amine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0043066	biological_process	negative regulation of apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue EDO A 401

Chain	Residue
A	PHE130
A	ILE133
A	ASP170
A	ASP234
A	GLY238

---

site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 402

Chain	Residue
A	LEU143
A	HOH509
A	ARG136
A	ALA138
A	LEU139
A	GLN140

---

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 403

Chain	Residue
A	ARG221
A	SER222
A	VAL225
A	ARG278
A	PRO279
A	HOH516

---

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 404

Chain	Residue
A	PHE100
A	GLU153
A	ASN160
A	GLN264
A	ARG268

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	VAL40
A	ILE66
A	HIS68

---

site_id	AC6
Number of Residues	2
Details	binding site for residue EDO A 406

Chain	Residue
A	ASP114
A	LEU193

---

site_id	AC7
Number of Residues	4
Details	binding site for residue EDO A 407

Chain	Residue
A	ASP170
A	GLU171
A	TYR207
A	ILE240

---

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO A 408

Chain	Residue
A	ARG214
A	HIS216

---

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO A 409

Chain	Residue
A	HIS265
A	HIS287
A	PRO288
A	EDO411

---

site_id	AD1
Number of Residues	2
Details	binding site for residue EDO A 410

Chain	Residue
A	LEU177
A	ASN178

---

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO A 411

Chain	Residue
A	GLU283
A	ASN286
A	HIS287
A	EDO409

---

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO A 412

Chain	Residue
A	HIS265
A	TRP269

---

site_id	AD4
Number of Residues	2
Details	binding site for residue EDO A 413

Chain	Residue
A	GLU142
A	ILE302

---

site_id	AD5
Number of Residues	5
Details	binding site for residue EDO A 414

Chain	Residue
A	TYR53
A	LYS194
A	GLY220
A	ARG221
A	HOH505

---

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO A 415

Chain	Residue
A	GLU141
A	GLU142

---

site_id	AD7
Number of Residues	8
Details	binding site for residue 6SN A 416

Chain	Residue
A	LEU44
A	ALA65
A	LYS67
A	GLU121
A	LEU174
A	ILE185
A	ASP186
A	HOH501

---

site_id	AD8
Number of Residues	6
Details	binding site for residue SO4 A 417

Chain	Residue
A	ARG156
A	ARG258
A	SER261
A	PHE281
A	HOH503
A	HOH538

---

site_id	AD9
Number of Residues	2
Details	binding site for residue SO4 A 418

Chain	Residue
A	ASP108
A	TRP109

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU44-LYS67

---

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

Chain	Residue	Details
A	VAL163-ILE175

---

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	ASP167

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU44

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862

Chain	Residue	Details
A	LYS67
A	GLU121
A	ASP128

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054

Chain	Residue	Details
A	SER98
A	SER261

---