Target Binding Site Detail

Target General Information

Target ID

T86528

Target Info

Target Name

Geranyltranstransferase (FDPS)

Synonyms

KIAA1293; Geranylgeranyl pyrophosphate synthase; Geranylgeranyl diphosphate synthase; GGPS1; GGPPSase; GGPP synthase; Farnesyltranstransferase; Farnesyl pyrophosphate synthase; Farnesyl diphosphate synthase; FPS protein; FPP synthase; Dimethylallyltranstransferase; (2E,6E)-farnesyl diphosphate synthase

Target Type

Successful Target

Gene Name

FDPS

Biochemical Class

Alkyl aryl transferase

UniProt ID

FPPS_HUMAN

Ligand General Information

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Ligand Name

Deuterium Oxide

Ligand Info

Canonical SMILES

InChI

1S/H2O/h1H2/i/hD2

InChIKey

XLYOFNOQVPJJNP-ZSJDYOACSA-N

PubChem Compound ID

24602

Drug Binding Sites of Target

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PDB ID: 5CG5 Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate

Method

X-ray diffraction

Resolution

1.40 Å

Mutation

[1]

PDB Sequence

DVYAQEKQDF

¹⁷

VQHFSQIVRV

²⁷

LTEDEMGHPE

³⁷

IGDAIARLKE

⁴⁷

VLEYNAIGGK

⁵⁷

YNRGLTVVVA

⁶⁷

FRELVEPRKQ

⁷⁷

DADSLQRAWT

⁸⁷

VGWCVELLQA

⁹⁷

FFLVADDIMD

¹⁰⁷

SSLTRRGQIC

¹¹⁷

WYQKPGVGLD

¹²⁷

AINDANLLEA

¹³⁷

CIYRLLKLYC

¹⁴⁷

REQPYYLNLI

¹⁵⁷

ELFLQSSYQT

¹⁶⁷

EIGQTLDLLT

¹⁷⁷

APQGNVDLVR

¹⁸⁷

FTEKRYKSIV

¹⁹⁷

KYKTAFYSFY

²⁰⁷

LPIAAAMYMA

²¹⁷

GIDGEKEHAN

²²⁷

AKKILLEMGE

²³⁷

FFQIQDDYLD

²⁴⁷

LFGDPSVTGK

²⁵⁷

IGTDIQDNKC

²⁶⁷

SWLVVQCLQR

²⁷⁷

ATPEQYQILK

²⁸⁷

ENYGQKEAEK

²⁹⁷

VARVKALYEE

³⁰⁷

LDLPAVFLQY

³¹⁷

EEDSYSHIMA

³²⁷

LIEQYAAPLP

³³⁷

PAVFLGLARK

³⁴⁷

IYK

Residue

Distance (Å)

ASP8

3.256

VAL9

2.649

TYR10

3.448

ALA11

2.269

GLN12

2.780

GLU13

2.453

LYS14

3.259

GLN15

2.305

ASP16

2.822

PHE17

3.710

VAL27

4.694

LEU28

2.516

THR29

4.420

ASP31

2.510

ASP40

2.839

ILE42

3.470

ALA43

2.680

ARG44

2.140

LEU45

3.113

LYS46

2.966

GLU47

2.805

VAL48

4.902

GLU50

3.064

TYR51

2.532

ASN52

1.994

ALA53

2.822

ILE54

2.230

GLY55

3.389

GLY56

2.368

LYS57

2.843

TYR58

2.346

ASN59

2.363

ARG60

2.060

GLY61

2.968

VAL65

2.668

VAL66

3.136

PHE68

3.776

ARG69

3.998

GLU70

1.809

ASP80

4.263

SER81

3.029

LEU82

4.496

ARG84

1.728

TRP86

2.154

TRP90

4.901

VAL92

4.953

GLU93

1.854

LEU94

4.580

LEU95

3.370

GLN96

2.187

ALA97

2.765

PHE98

3.496

PHE99

2.154

LEU100

3.386

VAL101

2.205

ALA102

2.461

ASP103

2.733

ASP104

1.775

ILE105

2.323

MET106

2.869

ASP107

2.040

SER108

2.433

SER109

1.820

LEU110

2.110

THR111

1.986

ARG112

2.292

ARG113

1.960

GLY114

2.887

GLN115

2.182

ILE116

3.582

CYS117

2.722

TRP118

2.254

TYR119

2.312

GLN120

2.037

LYS121

4.297

PRO122

4.293

GLY123

1.827

VAL124

1.980

GLY125

2.783

LEU126

2.058

ASP127

1.768

ALA128

4.022

ILE129

2.964

ASN130

1.851

ASP131

2.564

ALA132

2.780

ASN133

1.935

LEU134

3.191

GLU136

2.418

ALA137

2.035

CYS138

4.178

ILE139

4.326

TYR140

1.931

ARG141

2.103

LEU143

3.938

LYS144

2.537

TYR146

2.820

CYS147

4.824

GLN150

2.966

PRO151

2.246

TYR152

1.966

TYR153

2.641

LEU154

2.176

ASN155

2.044

LEU156

4.397

ILE157

3.477

GLU158

2.589

LEU159

2.844

PHE160

3.913

LEU161

2.844

GLN162

2.468

SER163

2.031

SER164

1.932

TYR165

4.024

GLN166

1.968

THR167

2.009

GLU168

1.671

GLN171

1.645

LEU173

3.414

Residue

Distance (Å)

ASP174

1.854

LEU175

2.949

LEU176

4.920

THR177

2.457

ALA178

2.281

PRO179

3.431

GLN180

2.538

GLY181

2.294

ASN182

4.374

VAL183

4.862

PHE188

3.105

THR189

2.778

GLU190

2.032

LYS191

2.511

ARG192

2.246

TYR193

2.912

LYS194

1.981

SER195

2.455

ILE196

2.858

VAL197

2.667

LYS198

2.547

TYR199

1.862

LYS200

2.171

THR201

2.734

ALA202

3.117

PHE203

2.493

TYR204

2.053

SER205

3.583

TYR207

2.771

LEU208

3.858

TYR215

2.070

MET216

3.566

ASP220

3.017

GLY221

4.410

GLU222

3.827

GLU224

4.325

HIS225

3.887

ALA226

2.783

ASN227

3.596

ALA228

3.412

LYS229

3.136

LYS230

2.767

ILE231

3.792

LEU233

2.254

GLU234

3.831

GLY236

4.392

GLU237

1.923

PHE238

4.832

PHE239

2.323

GLN240

1.864

GLN242

2.202

ASP243

1.956

ASP244

1.841

TYR245

3.794

LEU246

2.741

ASP247

1.832

LEU248

2.549

PHE249

4.798

GLY250

2.782

ASP251

1.985

PRO252

2.700

SER253

2.678

VAL254

3.311

THR255

1.895

GLY256

2.713

LYS257

2.359

ILE258

1.857

GLY259

2.218

THR260

1.879

ASP261

1.755

ILE262

2.427

GLN263

1.900

ASP264

2.300

ASN265

2.910

LYS266

2.223

CYS267

2.059

SER268

1.959

TRP269

4.604

LEU270

2.370

VAL271

3.001

VAL272

2.643

GLN273

4.932

LEU275

2.857

GLN276

1.980

ILE285

3.175

ASN289

2.497

TYR290

2.116

GLY291

2.655

GLN292

2.000

LYS293

2.614

GLU294

3.723

ALA295

2.716

GLU296

2.782

LYS297

3.894

VAL298

3.055

ALA299

2.872

ARG300

2.790

VAL301

4.509

ALA303

3.191

LEU304

3.352

TYR305

2.022

GLU307

4.930

ILE329

3.569

GLU330

2.841

GLN331

3.773

TYR332

2.948

ALA333

2.849

ALA334

2.218

PRO335

4.721

LEU336

3.131

PRO338

4.735

ALA339

2.059

VAL340

3.175

PHE341

2.891

LEU342

4.730

GLY343

2.665

LEU344

4.501

ARG346

2.848

LYS347

3.275

PDB ID: 5CG6 Neutron crystal structure of human farnesyl pyrophosphate synthase in complex with risedronate and isopentenyl pyrophosphate

Method

X-ray diffraction

Resolution

1.70 Å

Mutation

[1]

PDB Sequence

DVYAQEKQDF

¹⁷

VQHFSQIVRV

²⁷

LTEDEMGHPE

³⁷

IGDAIARLKE

⁴⁷

VLEYNAIGGK

⁵⁷

YNRGLTVVVA

⁶⁷

FRELVEPRKQ

⁷⁷

DADSLQRAWT

⁸⁷

VGWCVELLQA

⁹⁷

FFLVADDIMD

¹⁰⁷

SSLTRRGQIC

¹¹⁷

WYQKPGVGLD

¹²⁷

AINDANLLEA

¹³⁷

CIYRLLKLYC

¹⁴⁷

REQPYYLNLI

¹⁵⁷

ELFLQSSYQT

¹⁶⁷

EIGQTLDLLT

¹⁷⁷

APQGNVDLVR

¹⁸⁷

FTEKRYKSIV

¹⁹⁷

KYKTAFYSFY

²⁰⁷

LPIAAAMYMA

²¹⁷

GIDGEKEHAN

²²⁷

AKKILLEMGE

²³⁷

FFQIQDDYLD

²⁴⁷

LFGDPSVTGK

²⁵⁷

IGTDIQDNKC

²⁶⁷

SWLVVQCLQR

²⁷⁷

ATPEQYQILK

²⁸⁷

ENYGQKEAEK

²⁹⁷

VARVKALYEE

³⁰⁷

LDLPAVFLQY

³¹⁷

EEDSYSHIMA

³²⁷

LIEQYAAPLP

³³⁷

PAVFLGLARK

³⁴⁷

IYK

Residue

Distance (Å)

ARG44

2.208

GLU50

4.612

TYR51

2.087

ASN52

1.963

ALA53

2.690

ILE54

2.336

GLY55

3.601

GLY56

2.089

LYS57

2.520

TYR58

2.171

ASN59

2.176

ARG60

1.963

GLY61

3.693

TRP90

3.941

VAL92

4.839

GLU93

1.808

LEU94

4.324

LEU95

3.670

GLN96

2.504

ALA97

3.200

PHE98

3.626

PHE99

2.226

LEU100

3.589

VAL101

2.174

ALA102

3.125

ASP103

2.303

ASP104

1.769

ILE105

2.832

MET106

3.285

ASP107

2.197

SER108

4.805

SER109

1.706

LEU110

2.016

THR111

1.969

ARG112

2.040

ARG113

1.974

GLY114

3.870

GLN115

2.340

ILE116

4.309

CYS117

2.887

TRP118

2.194

TYR119

2.288

GLN120

2.089

LYS121

4.323

PRO122

4.369

GLY123

2.154

VAL124

2.061

GLY125

4.652

ASP127

2.107

ALA128

4.156

GLU136

2.107

ILE139

4.017

TYR140

1.875

PHE160

4.047

LEU161

2.852

SER163

3.887

SER164

2.428

GLN166

3.638

THR167

2.036

Residue

Distance (Å)

GLU168

1.668

GLN171

1.903

LEU173

4.307

ASP174

1.982

LEU175

2.112

THR177

2.262

ALA178

2.695

PHE188

4.348

TYR193

2.649

ILE196

2.776

VAL197

3.316

LYS198

3.971

TYR199

1.894

LYS200

1.971

THR201

3.655

ALA202

4.035

PHE203

2.522

TYR204

2.089

SER205

4.296

PHE238

4.849

PHE239

2.401

GLN240

2.741

GLN242

2.152

ASP243

2.069

ASP244

1.712

TYR245

3.738

LEU246

2.630

ASP247

1.938

LEU248

2.479

GLY250

3.619

ASP251

4.698

PRO252

2.682

SER253

4.621

THR255

1.839

GLY256

2.920

LYS257

1.668

ILE258

1.891

GLY259

2.637

THR260

1.959

ASP261

1.845

ILE262

2.028

GLN263

2.257

ASP264

3.046

ASN265

4.778

LYS266

2.335

CYS267

2.026

SER268

1.884

TRP269

4.033

LEU270

2.485

VAL271

2.384

TYR290

2.473

VAL298

2.648

VAL301

4.716

TYR305

1.876

ALA327

2.813

LEU328

4.802

GLU330

2.444

GLN331

3.149

References

Top

REF 1

Protonation State and Hydration of Bisphosphonate Bound to Farnesyl Pyrophosphate Synthase. J Med Chem. 2015 Sep 24;58(18):7549-56.

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