3ORK

Mycobacterium tuberculosis PknB kinase domain L33D mutant (crystal form 2)

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	32
Details	BINDING SITE FOR RESIDUE AGS A 340

Chain	Residue
A	LEU17
A	LYS40
A	MET92
A	GLU93
A	VAL95
A	THR99
A	LYS140
A	ALA142
A	ASN143
A	MET145
A	MET155
A	GLY18
A	ASP156
A	MN341
A	HOH342
A	TRS344
A	HOH359
A	HOH363
A	HOH387
A	HOH397
A	HOH401
A	HOH470
A	PHE19
A	HOH471
A	HOH602
A	HOH663
A	GLY20
A	GLY21
A	MET22
A	SER23
A	VAL25
A	ALA38

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 341

Chain	Residue
A	ASN143
A	ASP156
A	AGS340
A	HOH359
A	HOH363

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 343

Chain	Residue
A	ARG35
A	ARG189
A	ARG230

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS A 344

Chain	Residue
A	GLY18
A	PHE19
A	ARG48
A	ARG101
A	ASP102
A	AGS340
A	HOH400
A	HOH401
A	HOH427
A	HOH501

---

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

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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

---

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

---

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	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12548283

Chain	Residue	Details
A	SER169
A	SER295

---

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

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:12548283, ECO:0000269|PubMed:15967413

Chain	Residue	Details
A	THR294

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