5U94

Crystal structure of the Mycobacterium tuberculosis PASTA kinase PknB in complex with the potential theraputic kinase inhibitor GSK690693.

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	13
Details	binding site for residue G93 A 301

Chain	Residue
A	PHE19
A	ASP156
A	PHE157
A	MG310
A	HOH433
A	VAL25
A	LYS40
A	GLU59
A	VAL72
A	MET92
A	GLU93
A	VAL95
A	MET155

---

site_id	AC2
Number of Residues	3
Details	binding site for residue GOL A 302

Chain	Residue
A	VAL250
A	ASP272
A	HOH410

---

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 303

Chain	Residue
A	PHE216
A	THR217
A	GLN227
A	ARG239

---

site_id	AC4
Number of Residues	3
Details	binding site for residue GOL A 304

Chain	Residue
A	THR179
A	ALA180
A	GLN181

---

site_id	AC5
Number of Residues	4
Details	binding site for residue GOL A 305

Chain	Residue
A	VAL98
A	GLU107
A	ILE146
A	GOL306

---

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 306

Chain	Residue
A	ARG114
A	ILE146
A	ASN150
A	GOL305

---

site_id	AC7
Number of Residues	2
Details	binding site for residue GOL A 307

Chain	Residue
A	ASP36
A	HOH404

---

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL A 308

Chain	Residue
A	PRO109
A	MET110
A	THR111
A	HIS240

---

site_id	AC9
Number of Residues	9
Details	binding site for residue GOL A 309

Chain	Residue
A	ASN67
A	ASN67
A	HIS68
A	PRO69
A	PRO69
A	LYS153
A	HOH408
A	HOH408
A	HOH409

---

site_id	AD1
Number of Residues	3
Details	binding site for residue MG A 310

Chain	Residue
A	ASN143
A	ASP156
A	G93301

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU17-LYS40

---

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

Chain	Residue	Details
A	ILE134-ILE146

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP138

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895

Chain	Residue	Details
A	LYS40
A	GLU93
A	LYS140
A	LEU17

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	ASN143
A	ASP156

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609

Chain	Residue	Details
A	THR2

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413

Chain	Residue	Details
A	SER166

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283

Chain	Residue	Details
A	SER169

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609, ECO:0000269|PubMed:19008858

Chain	Residue	Details
A	THR171

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:15985609

Chain	Residue	Details
A	THR173

---