1O6Y

Catalytic domain of PknB kinase from Mycobacterium tuberculosis

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	5
Details	BINDING SITE FOR RESIDUE MG A 1280

Chain	Residue
A	ASN143
A	ASP156
A	ACP1279
A	HOH2079
A	HOH2080

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1281

Chain	Residue
A	HOH2081
A	HOH2082
A	LYS40
A	ACP1279
A	HOH2054
A	HOH2055

---

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ACP A 1279

Chain	Residue
A	GLY18
A	GLY20
A	GLY21
A	MET22
A	SER23
A	ALA38
A	LYS40
A	VAL72
A	GLU93
A	VAL95
A	THR99
A	ALA142
A	ASN143
A	ASP156
A	MG1280
A	MG1281
A	HOH2054
A	HOH2055
A	HOH2079
A	HOH2080
A	HOH2081
A	HOH2082
A	HOH2083
A	HOH2084

---

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

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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

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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	LEU17
A	LYS40
A	GLU93
A	LYS140

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	ASN143
A	ASP156

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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

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ALA142
A	ASP138

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP138
A	LYS140

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP138
A	ASN143
A	LYS140

---