Binding Site Information of Target

Target General Information

Top

Target ID

T91895

Target Info

Target Name

Bacterial Pantothenate kinase (Bact coaA)

Synonyms

Rts protein; Pantothenic acid kinase; Pantothenate kinase

Target Type

Literature-reported Target

Gene Name

Bact coaA

Biochemical Class

Kinase

UniProt ID

COAA_ECOLI

Drug Binding Sites of Target

Top

Ligand Name: Pantothenic acid

Ligand Info

Structure Description

Crystal Structure of E. coli Pantothenate kinase

PDB:1SQ5

Method

X-ray diffraction

Resolution

2.20 Å

Mutation

[1]

PDB Sequence

MTPYLQFDRN

¹⁰¹⁸

QWAALRDMLS

¹⁰³²

EDEIARLKGI

¹⁰⁴²

NEDLSLEEVA

¹⁰⁵²

EIYLPLSRLL

¹⁰⁶²

NFYISSNLRR

¹⁰⁷²

QAVLEQFLGT

¹⁰⁸²

NQRIPYIISI

¹⁰⁹³

AGSVAVGKST

¹¹⁰³

TARVLQALLS

¹¹¹³

RWPEHRRVEL

¹¹²³

ITTDGFLHPN

¹¹³³

QVLKERGLMK

¹¹⁴³

KKGFPESYDM

¹¹⁵³

HRLVKFVSDL

¹¹⁶³

KSGVPNVTAP

¹¹⁷³

VYSHLIYDVI

¹¹⁸³

PDGDKTVVPD

¹¹⁹⁴

ILILEGLNVL

¹²⁰⁴

QSGMDYPHDP

¹²¹⁴

HHVFVSDFVD

¹²²⁴

FSIYVDAPED

¹²³⁴

LLQTWYINRF

¹²⁴⁴

LKFREGAFTD

¹²⁵⁴

PDSYFHNYAK

¹²⁶⁴

LTKEEAIKTA

¹²⁷⁴

MTLWKEINWL

¹²⁸⁴

NLKQNILPTR

¹²⁹⁴

ERASLILTKS

¹³⁰⁴

ANHAVEEVRL

¹³¹⁴

Residue

Distance (Å)

VAL1097

4.094

ASP1127

2.800

LEU1130

3.773

LYS1145

3.339

GLY1146

3.366

TYR1151

4.257

TYR1175

4.548

HIS1177

3.062

Residue

Distance (Å)

TYR1180

4.174

LEU1201

3.638

TYR1240

2.627

ARG1243

4.898

LEU1277

4.006

ILE1281

3.602

ASN1282

2.741

Ligand Name: Coenzyme A

Ligand Info

Structure Description

STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A

PDB:1ESM

Method

X-ray diffraction

Resolution

2.50 Å

Mutation

Yes

[2]

PDB Sequence

QTLTPYLQFD

¹⁶

RNQWAALRDS

²⁶

VPTLSEDEIA

³⁷

RLKGINEDLS

⁴⁷

LEEVAEIYLP

⁵⁷

LSRLLNFYIS

⁶⁷

SNLRRQAVLE

⁷⁷

QFLGTNGQRI

⁸⁷

PYIISIAGSV

⁹⁷

AVGKSTTARV

¹⁰⁷

LQALLSRWPE

¹¹⁷

HRRVELITTD

¹²⁷

GFLHPNQVLK

¹³⁷

ERGLKKKGFP

¹⁴⁸

ESYDHRLVKF

¹⁵⁹

VSDLKSGVPN

¹⁶⁹

VTAPVYSHLI

¹⁷⁹

YDVIPDGDKT

¹⁸⁹

VVQPDILILE

¹⁹⁹

GLNVLQSGDY

²¹⁰

PHDPHHVFVS

²²⁰

DFVDFSIYVD

²³⁰

APEDLLQTWY

²⁴⁰

INRFLKFREG

²⁵⁰

AFTDPDSYFH

²⁶⁰

NYAKLTKEEA

²⁷⁰

IKTATLWKEI

²⁸¹

NWLNLKQNIL

²⁹¹

PTRERASLIL

³⁰¹

TKSANHAVEE

³¹¹

VRLRK

Residue

Distance (Å)

GLY41

3.381

ILE42

2.847

GLY95

4.843

SER96

4.489

VAL97

3.222

ALA98

3.426

VAL99

4.873

GLY100

4.990

LYS101

3.135

SER102

2.729

THR103

4.638

ARG106

2.555

ASP127

4.871

LEU130

4.407

LYS145

3.318

GLY146

4.250

TYR151

4.501

Residue

Distance (Å)

TYR175

3.647

HIS177

3.207

TYR180

3.127

GLU199

4.223

GLY200

4.519

LEU201

3.292

TYR240

2.507

ARG243

3.122

PHE244

3.924

PHE247

3.426

ALA251

4.205

PHE252

3.664

PHE259

3.722

TYR262

4.101

LEU277

3.871

ILE281

4.046

ASN282

3.076

Ligand Name: AMP-PNP

Ligand Info

Structure Description

STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A

PDB:1ESN

Method

X-ray diffraction

Resolution

2.60 Å

Mutation

Yes

[2]

PDB Sequence

QTLTPYLQFD

¹⁶

RNQWAALRDS

²⁶

VPTLSEDEIA

³⁷

RLKGINEDLS

⁴⁷

LEEVAEIYLP

⁵⁷

LSRLLNFYIS

⁶⁷

SNLRRQAVLE

⁷⁷

QFLGTNGQRI

⁸⁷

PYIISIAGSV

⁹⁷

AVGKSTTARV

¹⁰⁷

LQALLSRWPE

¹¹⁷

HRRVELITTD

¹²⁷

GFLHPNQVLK

¹³⁷

ERGLKKKGFP

¹⁴⁸

ESYDHRLVKF

¹⁵⁹

VSDLKSGVPN

¹⁶⁹

VTAPVYSHLI

¹⁷⁹

YDVIPDGDKT

¹⁸⁹

VVQPDILILE

¹⁹⁹

GLNVLQSGDY

²¹⁰

PHDPHHVFVS

²²⁰

DFVDFSIYVD

²³⁰

APEDLLQTWY

²⁴⁰

INRFLKFREG

²⁵⁰

AFTDPDSYFH

²⁶⁰

NYAKLTKEEA

²⁷⁰

IKTATLWKEI

²⁸¹

NWLNLKQNIL

²⁹¹

PTRERASLIL

³⁰¹

TKSANHAVEE

³¹¹

VRLRK

Click to Show 3D Structure of This Binding Site

set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:43 or .A:45 or .A:46 or .A:50 or .A:55 or .A:96 or .A:97 or .A:98 or .A:99 or .A:100 or .A:101 or .A:102 or .A:103 or .A:104 or .A:127 or .A:199 or .A:201 or .A:243 or .A:303 or .A:306 or .A:307; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all

Residue

Distance (Å)

ASN43

3.474

ASP45

3.371

LEU46

3.358

GLU50

4.882

TYR55

3.329

SER96

4.108

VAL97

3.294

ALA98

2.852

VAL99

3.105

GLY100

2.929

LYS101

2.887

Residue

Distance (Å)

SER102

2.690

THR103

2.597

THR104

4.901

ASP127

4.512

GLU199

3.469

LEU201

4.365

ARG243

3.120

LYS303

3.232

ASN306

4.386

HIS307

3.384

Ligand Name: adenosine diphosphate

Ligand Info

Structure Description

Crystal Structure of E. coli Pantothenate kinase

PDB:1SQ5

Method

X-ray diffraction

Resolution

2.20 Å

Mutation

[1]

PDB Sequence

MTPYLQFDRN

¹⁰¹⁸

QWAALRDMLS

¹⁰³²

EDEIARLKGI

¹⁰⁴²

NEDLSLEEVA

¹⁰⁵²

EIYLPLSRLL

¹⁰⁶²

NFYISSNLRR

¹⁰⁷²

QAVLEQFLGT

¹⁰⁸²

NQRIPYIISI

¹⁰⁹³

AGSVAVGKST

¹¹⁰³

TARVLQALLS

¹¹¹³

RWPEHRRVEL

¹¹²³

ITTDGFLHPN

¹¹³³

QVLKERGLMK

¹¹⁴³

KKGFPESYDM

¹¹⁵³

HRLVKFVSDL

¹¹⁶³

KSGVPNVTAP

¹¹⁷³

VYSHLIYDVI

¹¹⁸³

PDGDKTVVPD

¹¹⁹⁴

ILILEGLNVL

¹²⁰⁴

QSGMDYPHDP

¹²¹⁴

HHVFVSDFVD

¹²²⁴

FSIYVDAPED

¹²³⁴

LLQTWYINRF

¹²⁴⁴

LKFREGAFTD

¹²⁵⁴

PDSYFHNYAK

¹²⁶⁴

LTKEEAIKTA

¹²⁷⁴

MTLWKEINWL

¹²⁸⁴

NLKQNILPTR

¹²⁹⁴

ERASLILTKS

¹³⁰⁴

ANHAVEEVRL

¹³¹⁴

Click to Show 3D Structure of This Binding Site

set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ADP or .ADP2 or .ADP3 or :3ADP;style chemicals stick;color identity;select .A:1043 or .A:1045 or .A:1046 or .A:1047 or .A:1055 or .A:1096 or .A:1097 or .A:1098 or .A:1099 or .A:1100 or .A:1101 or .A:1102 or .A:1103 or .A:1199 or .A:1239 or .A:1243 or .A:1303 or .A:1306 or .A:1307; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all

Residue

Distance (Å)

ASN1043

2.779

ASP1045

3.511

LEU1046

3.506

SER1047

4.895

TYR1055

4.124

SER1096

3.634

VAL1097

4.012

ALA1098

2.957

VAL1099

3.326

GLY1100

2.983

Residue

Distance (Å)

LYS1101

2.760

SER1102

2.819

THR1103

3.142

GLU1199

4.252

TRP1239

4.373

ARG1243

2.861

LYS1303

2.983

ASN1306

4.806

HIS1307

3.218

Ligand Name: Selenomethionine

Ligand Info

Structure Description

STRUCTURAL BASIS FOR THE FEEDBACK REGULATION OF ESCHERICHIA COLI PANTOTHENATE KINASE BY COENZYME A

PDB:1ESM

Method

X-ray diffraction

Resolution

2.50 Å

Mutation

Yes

[2]

PDB Sequence

QTLTPYLQFD

¹⁶

RNQWAALRDS

²⁶

VPTLSEDEIA

³⁷

RLKGINEDLS

⁴⁷

LEEVAEIYLP

⁵⁷

LSRLLNFYIS

⁶⁷

SNLRRQAVLE

⁷⁷

QFLGTNGQRI

⁸⁷

PYIISIAGSV

⁹⁷

AVGKSTTARV

¹⁰⁷

LQALLSRWPE

¹¹⁷

HRRVELITTD

¹²⁷

GFLHPNQVLK

¹³⁷

ERGLKKKGFP

¹⁴⁸

ESYDHRLVKF

¹⁵⁹

VSDLKSGVPN

¹⁶⁹

VTAPVYSHLI

¹⁷⁹

YDVIPDGDKT

¹⁸⁹

VVQPDILILE

¹⁹⁹

GLNVLQSGDY

²¹⁰

PHDPHHVFVS

²²⁰

DFVDFSIYVD

²³⁰

APEDLLQTWY

²⁴⁰

INRFLKFREG

²⁵⁰

AFTDPDSYFH

²⁶⁰

NYAKLTKEEA

²⁷⁰

IKTATLWKEI

²⁸¹

NWLNLKQNIL

²⁹¹

PTRERASLIL

³⁰¹

TKSANHAVEE

³¹¹

VRLRK

Click to Show 3D Structure of This Binding Site

set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:6 or .A:7 or .A:8 or .A:10 or .A:11 or .A:24 or .A:27 or .A:28 or .A:30 or .A:31 or .A:36 or .A:48 or .A:51 or .A:52 or .A:56 or .A:111 or .A:133 or .A:136 or .A:137 or .A:140 or .A:141 or .A:143 or .A:144 or .A:145 or .A:151 or .A:152 or .A:154 or .A:155 or .A:156 or .A:157 or .A:158 or .A:180 or .A:202 or .A:205 or .A:206 or .A:207 or .A:209 or .A:210 or .A:211 or .A:218 or .A:219 or .A:237 or .A:241 or .A:258 or .A:270 or .A:271 or .A:272 or .A:273 or .A:274 or .A:276 or .A:277 or .A:278 or .A:279 or .A:280 or .A:281 or .A:296 or .A:316; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all

Residue

Distance (Å)

GLN6

3.954

THR7

2.805

LEU8

1.328

THR10

1.322

PRO11

4.309

ARG24

3.832

VAL27

4.107

PRO28

1.328

THR30

1.318

LEU31

3.004

ILE36

4.415

LEU48

4.611

VAL51

3.110

ALA52

4.893

LEU56

3.769

LEU111

3.664

ASN133

3.364

LEU136

3.733

LYS137

3.494

GLY140

3.706

LEU141

1.322

LYS143

1.323

LYS144

2.926

LYS145

4.046

TYR151

3.210

ASP152

1.329

HIS154

1.323

ARG155

2.900

LEU156

3.186

Residue

Distance (Å)

VAL157

2.848

LYS158

4.505

TYR180

3.683

ASN202

2.796

GLN205

4.868

SER206

3.097

GLY207

1.332

ASP209

1.326

TYR210

2.927

PRO211

4.137

PHE218

4.312

VAL219

3.558

GLN237

2.901

ILE241

3.809

TYR258

3.692

ALA270

4.814

ILE271

2.976

LYS272

3.326

THR273

3.332

ALA274

1.339

THR276

1.328

LEU277

3.099

TRP278

3.087

LYS279

2.736

GLU280

4.578

ILE281

4.766

ARG296

3.450

LYS316

4.909

Click to View More Binding Site Information of This Target and Ligand Pair

References

Top

REF 1

The structure of the pantothenate kinase.ADP.pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolites. J Biol Chem. 2004 Aug 20;279(34):35622-9.

REF 2

Structural basis for the feedback regulation of Escherichia coli pantothenate kinase by coenzyme A. J Biol Chem. 2000 Sep 8;275(36):28093-9.

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