Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ORI

Mycobacterium tuberculosis PknB kinase domain L33D mutant (crystal form 1)

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
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AGS A 340

Chain	Residue
A	GLY18
A	GLU93
A	VAL95
A	LYS140
A	ASN143
A	MET145
A	ASP156
A	MN341
A	MN342
A	HOH505
A	HOH551
A	GLY20
A	HOH592
A	HOH818
A	HOH897
A	GLY21
A	MET22
A	SER23
A	VAL25
A	ALA38
A	LYS40
A	MET92

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 341

Chain	Residue
A	ASP156
A	AGS340
A	HOH897
A	HOH898

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN A 342

Chain	Residue
A	ASN143
A	ASP156
A	AGS340

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE AGS B 440

Chain	Residue
B	GLY18
B	GLY20
B	GLY21
B	MET22
B	SER23
B	VAL25
B	ALA38
B	LYS40
B	MET92
B	GLU93
B	VAL95
B	LYS140
B	ASN143
B	MET145
B	MET155
B	ASP156
B	MN441
B	MN442
B	HOH550
B	HOH608
B	HOH666
B	HOH842

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 441

Chain	Residue
B	ASP156
B	AGS440
B	HOH842
B	HOH843

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MN B 442

Chain	Residue
B	ASN143
B	ASP156
B	AGS440

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE AGS C 540

Chain	Residue
C	GLY18
C	GLY20
C	GLY21
C	MET22
C	SER23
C	VAL25
C	ALA38
C	LYS40
C	MET92
C	GLU93
C	VAL95
C	THR99
C	LYS140
C	ALA142
C	ASN143
C	MET145
C	MET155
C	ASP156
C	GLY178
C	HOH392
C	HOH393
C	HOH458
C	MN541
C	MN542
C	HOH547
C	HOH624
C	HOH748

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 541

Chain	Residue
C	GLU59
C	ASP156
C	HOH356
C	AGS540

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 542

Chain	Residue
C	ASN143
C	ASP156
C	AGS540
C	HOH624

site_id	BC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE AGS D 640

Chain	Residue
D	ALA38
D	LYS40
D	VAL72
D	MET92
D	GLU93
D	VAL95
D	THR99
D	LYS140
D	ALA142
D	ASN143
D	MET145
D	MET155
D	ASP156
D	HOH349
D	HOH378
D	HOH380
D	HOH451
D	HOH471
D	HOH630
D	MN641
D	MN642
D	HOH668
D	GLY18
D	GLY20
D	GLY21
D	MET22
D	SER23
D	VAL25

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 641

Chain	Residue
D	GLU59
D	ASP156
D	HOH321
D	AGS640

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 642

Chain	Residue
D	ASN143
D	ASP156
D	HOH349
D	AGS640

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. IiHrDVKpaNIMI

Chain	Residue	Details
A	ILE134-ILE146

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP138
B	ASP138
C	ASP138
D	ASP138

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000269\|PubMed:12548283, ECO:0000269\|PubMed:12551895

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

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	ASN143
A	ASP156
B	ASN143
B	ASP156
C	ASN143
C	ASP156
D	ASN143
D	ASP156

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N-acetylthreonine => ECO:0007744\|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:12548283, ECO:0000269\|PubMed:15967413

Chain	Residue	Details
A	SER166
B	SER166
C	SER166
D	SER166

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:12548283

Chain	Residue	Details
A	SER169
A	SER295
B	SER169
B	SER295
C	SER169
C	SER295
D	SER169
D	SER295

site_id	SWS_FT_FI7
Number of Residues	4
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
B	THR171
C	THR171
D	THR171

site_id	SWS_FT_FI8
Number of Residues	4
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
C	THR173
D	THR173

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269\|PubMed:12548283, ECO:0000269\|PubMed:15967413

Chain	Residue	Details
A	THR294
B	THR294
C	THR294
D	THR294

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)