Prosaposin

Peptide B accession

Peptide A residue number

445

Peptide B residue number

484

Ligandability

Cysteine 445 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 484 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 241 and 241 (47 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin b

Structure deposition date

2002-11-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

241

Peptide B residue number

241

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 106 and 106 (47 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7p4t

Structure name

tetrameric structure of murine sapa

Structure deposition date

2021-07-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

106

Peptide B residue number

106

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 509 and 484 (72 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5u85

Structure name

murine saposin-d (sapd), open conformation

Structure deposition date

2016-12-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

509

Peptide B residue number

484

Ligandability

Cysteine 509 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 484 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 357 and 318 (47 and 8 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2z9a

Structure name

crystal structure of human saposin c dimer in open conformation

Structure deposition date

2007-09-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

357

Peptide B residue number

318

Ligandability

Cysteine 357 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 318 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 201 and 201 (7 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4v2o

Structure name

structure of saposin b in complex with chloroquine

Structure deposition date

2014-10-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

201

Peptide B residue number

201

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Prosaposin at cysteines 66 and 66 (7 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5nxb

Structure name

mouse galactocerebrosidase in complex with saposin a

Structure deposition date

2017-05-09

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Prosaposin

Peptide B name

Prosaposin

Peptide A accession

Peptide B accession

Peptide A residue number

Peptide B residue number

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 315 and 388 (5 and 78 respectively in this structure).

Details

Redox score ?

PDB code

2gtg

Structure name

crystal structure of human saposin c

Structure deposition date

2006-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

315

Residue number B

388

Peptide name

Prosaposin

Ligandability

Cysteine 315 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 388 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 63 and 138 (4 and 79 respectively in this structure).

Details

Redox score ?

PDB code

4uex

Structure name

structure of human saposin a at lysosomal ph

Structure deposition date

2014-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

138

Peptide name

Prosaposin

Ligandability

Cysteine 63 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 138 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 346 and 357 (36 and 47 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

orthorhombic crystal structure of human saposin c dimer in open conformation

Structure deposition date

2007-08-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

346

Residue number B

357

Peptide name

Prosaposin

Ligandability

Cysteine 346 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 357 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 409 and 482 (5 and 78 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin d (triclinic)

Structure deposition date

2007-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

409

Residue number B

482

Peptide name

Prosaposin

Ligandability

Cysteine 409 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 482 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 94 and 106 (35 and 47 respectively in this structure).

Details

Redox score ?

PDB code

4uex

Structure name

structure of human saposin a at lysosomal ph

Structure deposition date

2014-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

106

Peptide name

Prosaposin

Ligandability

Cysteine 94 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 106 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 66 and 132 (7 and 73 respectively in this structure).

Details

Redox score ?

PDB code

4ddj

Structure name

crystal structure of saposin a in complex with lauryldimethylamine-n- oxide (ldao)

Structure deposition date

2012-01-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

132

Peptide name

Prosaposin

Ligandability

Cysteine 66 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 132 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 440 and 451 (36 and 47 respectively in this structure).

Details

Redox score ?

PDB code

2r0r

Structure name

crystal structure of human saposin d variant sapd k9e

Structure deposition date

2007-08-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

440

Residue number B

451

Peptide name

Prosaposin

Ligandability

Cysteine 440 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 451 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 230 and 241 (36 and 47 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin b

Structure deposition date

2002-11-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

230

Residue number B

241

Peptide name

Prosaposin

Ligandability

Cysteine 230 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 241 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 318 and 382 (8 and 72 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

orthorhombic crystal structure of human saposin c dimer in open conformation

Structure deposition date

2007-08-15

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

318

Residue number B

382

Peptide name

Prosaposin

Ligandability

Cysteine 318 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 382 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 198 and 271 (4 and 77 respectively in this structure).

Details

Redox score ?

PDB code

4v2o

Structure name

structure of saposin b in complex with chloroquine

Structure deposition date

2014-10-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

198

Residue number B

271

Peptide name

Prosaposin

Ligandability

Cysteine 198 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 271 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 412 and 476 (8 and 72 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin d (triclinic)

Structure deposition date

2007-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

412

Residue number B

476

Peptide name

Prosaposin

Ligandability

Cysteine 412 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 476 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 201 and 265 (7 and 71 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin b

Structure deposition date

2002-11-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

201

Residue number B

265

Peptide name

Prosaposin

Ligandability

Cysteine 201 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 265 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 382 and 388 (72 and 78 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

orthorhombic crystal structure of human saposin c dimer in open conformation

Structure deposition date

2007-08-15

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

382

Residue number B

388

Peptide name

Prosaposin

Ligandability

Cysteine 382 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 388 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 132 and 138 (73 and 79 respectively in this structure).

Details

Redox score ?

PDB code

2dob

Structure name

crystal structure of human saposin a

Structure deposition date

2006-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

132

Residue number B

138

Peptide name

Prosaposin

Ligandability

Cysteine 132 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 138 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 265 and 271 (71 and 77 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin b

Structure deposition date

2002-11-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

265

Residue number B

271

Peptide name

Prosaposin

Ligandability

Cysteine 265 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 271 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 476 and 482 (72 and 78 respectively in this structure).

Details

Redox score ?

PDB code

3bqp

Structure name

crystal structure of human saposin d (orthorhombic)

Structure deposition date

2007-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

476

Residue number B

482

Peptide name

Prosaposin

Ligandability

Cysteine 476 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 482 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 318 and 388 (8 and 78 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

orthorhombic crystal structure of human saposin c dimer in open conformation

Structure deposition date

2007-08-15

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

318

Residue number B

388

Peptide name

Prosaposin

Ligandability

Cysteine 318 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 388 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 66 and 138 (7 and 79 respectively in this structure).

Details

Redox score ?

PDB code

2dob

Structure name

crystal structure of human saposin a

Structure deposition date

2006-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

138

Peptide name

Prosaposin

Ligandability

Cysteine 66 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 138 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 201 and 271 (7 and 77 respectively in this structure).

Details

Redox score ?

PDB code

6slr

Structure name

structure of saposin b in complex with atovaquone

Structure deposition date

2019-08-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

201

Residue number B

271

Peptide name

Prosaposin

Ligandability

Cysteine 201 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 271 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 412 and 482 (8 and 78 respectively in this structure).

Details

Redox score ?

PDB code

2r0r

Structure name

crystal structure of human saposin d variant sapd k9e

Structure deposition date

2007-08-21

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

412

Residue number B

482

Peptide name

Prosaposin

Ligandability

Cysteine 412 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 482 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 63 and 132 (4 and 73 respectively in this structure).

Details

Redox score ?

PDB code

4ddj

Structure name

crystal structure of saposin a in complex with lauryldimethylamine-n- oxide (ldao)

Structure deposition date

2012-01-18

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

132

Peptide name

Prosaposin

Ligandability

Cysteine 63 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 132 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 315 and 382 (5 and 72 respectively in this structure).

Details

Redox score ?

PDB code

2gtg

Structure name

crystal structure of human saposin c

Structure deposition date

2006-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

315

Residue number B

382

Peptide name

Prosaposin

Ligandability

Cysteine 315 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 382 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 198 and 265 (4 and 71 respectively in this structure).

Details

Redox score ?

PDB code

6slr

Structure name

structure of saposin b in complex with atovaquone

Structure deposition date

2019-08-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

198

Residue number B

265

Peptide name

Prosaposin

Ligandability

Cysteine 198 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 265 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 409 and 476 (5 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin d (triclinic)

Structure deposition date

2007-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

409

Residue number B

476

Peptide name

Prosaposin

Ligandability

Cysteine 409 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 476 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 315 and 318 (5 and 8 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

2gtg

Structure name

crystal structure of human saposin c

Structure deposition date

2006-04-28

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

315

Residue number B

318

Peptide name

Prosaposin

Ligandability

Cysteine 315 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 318 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 409 and 412 (5 and 8 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin d (triclinic)

Structure deposition date

2007-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

409

Residue number B

412

Peptide name

Prosaposin

Ligandability

Cysteine 409 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 412 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 63 and 66 (4 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4uex

Structure name

structure of human saposin a at lysosomal ph

Structure deposition date

2014-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

Residue number B

Peptide name

Prosaposin

Ligandability

Cysteine 63 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 66 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Prosaposin between cysteines 198 and 201 (4 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

Structure name

crystal structure of human saposin b

Structure deposition date

2002-11-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

198

Residue number B

201

Peptide name

Prosaposin

Ligandability

Cysteine 198 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.

Cysteine 201 of Prosaposin

Not ligandable in the dataset of Vinogradova et al.