3F69

Crystal structure of the Mycobacterium tuberculosis PknB mutant kinase domain in complex with KT5720

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE XDR A 309

Chain	Residue
A	LEU17
A	VAL155
A	GLY18
A	VAL25
A	ALA38
A	GLU93
A	VAL95
A	GLY97
A	ALA142
A	ASN143

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 310

Chain	Residue
A	ARG10
A	ARG32

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 311

Chain	Residue
A	ALA256
A	LYS257
A	ASN258
A	ASN261

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE XDR B 309

Chain	Residue
B	LEU17
B	GLY18
B	ALA38
B	LYS40
B	GLU93
B	VAL95
B	THR99
B	ALA142
B	ASN143
B	LEU145
B	VAL155
B	ASP156

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 310

Chain	Residue
B	ARG32

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 311

Chain	Residue
B	ALA256
B	LYS257
B	ASN258
B	ASN261

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE134-ILE146

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP138
B	ASP138

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:12551895

Chain	Residue	Details
A	LEU17
A	GLU93
A	LYS140
B	LEU17
B	LYS40
B	GLU93
B	LYS140
A	LYS40

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	ASN143
A	ASP156
B	ASN143
B	ASP156

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413

Chain	Residue	Details
A	SER166
B	SER166

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283

Chain	Residue	Details
B	SER169
B	SER295
A	SER169
A	SER295

---

site_id	SWS_FT_FI7
Number of Residues	2
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	TPO171
B	TPO171

---

site_id	SWS_FT_FI8
Number of Residues	2
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
B	THR173

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413

Chain	Residue	Details
A	THR294
B	THR294

---