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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FUM

Catalytic domain of protein kinase PknB from Mycobacterium tuberculosis in complex with mitoxantrone

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	13
Details	BINDING SITE FOR RESIDUE MIX A 539

Chain	Residue
A	LEU17
A	ALA142
A	ASN143
A	MET145
B	ASP219
A	PHE19
A	ALA38
A	GLU93
A	TYR94
A	VAL95
A	GLY97
A	ASP102
A	LYS140

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MIX B 1539

Chain	Residue
A	ASP219
B	LEU17
B	GLY18
B	PHE19
B	ALA38
B	GLU93
B	TYR94
B	VAL95
B	GLY97
B	LYS140
B	ASN143
B	MET145
B	ASP156

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MIX C 2539

Chain	Residue
C	LEU17
C	PHE19
C	ALA38
C	MET92
C	GLU93
C	VAL95
C	GLY97
C	ASN143
C	MET155
C	ASP156

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MIX D 3539

Chain	Residue
D	LEU17
D	GLY18
D	PHE19
D	VAL25
D	ALA38
D	MET92
D	VAL95
D	GLY97
D	VAL98
D	ASP138
D	ASN143
D	MET145
D	MET155
D	ASP156

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	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
C	LYS40
C	GLU93
C	LYS140
D	LEU17
D	LYS40
D	GLU93
D	LYS140
A	LYS40
A	GLU93
A	LYS140
B	LEU17
B	LYS40
B	GLU93
B	LYS140
C	LEU17

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	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:12548283

Chain	Residue	Details
A	SER169
B	SER169
C	SER169
D	SER169

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

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

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	THR179
B	ASP138
B	LYS140

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	THR179
D	ASP138
D	LYS140

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP138
A	ASN143
A	LYS140

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP138
B	ASN143
B	LYS140

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP138
C	ASN143
C	LYS140

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP138
D	ASN143
D	LYS140

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

Chain	Residue	Details
B	ALA142
B	ASP138

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ALA142
C	ASP138

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ALA142
D	ASP138

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP138
A	LYS140

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP138
B	LYS140

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP138
C	LYS140

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP138
D	LYS140

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	THR179
A	ASP138
A	LYS140

224004

PDB entries from 2024-08-21

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