Pappalysin-1

Peptide A residue number

169

Peptide B residue number

732

Ligandability

Cysteine 169 of Bone marrow proteoglycan

Not ligandable in the dataset of Vinogradova et al.

Cysteine 732 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 732 of Pappalysin-1 and cysteine 120 of Stanniocalcin-2 (652 and 120 respectively in this structure).

Details

Redox score ?

PDB code

7y5q

Structure name

structure of 1:1 papp-a

Structure deposition date

2022-06-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Pappalysin-1

Peptide B name

Stanniocalcin-2

Peptide A accession

Peptide B accession

O76061

Peptide A residue number

732

Peptide B residue number

120

Ligandability

Cysteine 732 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 120 of Stanniocalcin-2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Pappalysin-1 at cysteines 1210 and 1210 (1130 and 1130 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

cryo-em structure of substrate unbound papp-a

Structure deposition date

2022-06-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Pappalysin-1

Peptide B name

Pappalysin-1

Peptide A accession

Peptide B accession

Peptide A residue number

1210

Peptide B residue number

1210

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1215 and 1269 (1135 and 1189 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1215

Residue number B

1269

Peptide name

Pappalysin-1

Ligandability

Cysteine 1215 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1269 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1442 and 1471.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1442

Residue number B

1471

Peptide name

Pappalysin-1

Ligandability

Cysteine 1442 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1471 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1600 and 1606 (1520 and 1526 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1600

Residue number B

1606

Peptide name

Pappalysin-1

Ligandability

Cysteine 1600 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1606 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1415 and 1458 (1335 and 1378 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1415

Residue number B

1458

Peptide name

Pappalysin-1

Ligandability

Cysteine 1415 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1458 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1492 and 1502.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1492

Residue number B

1502

Peptide name

Pappalysin-1

Ligandability

Cysteine 1492 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1502 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 713 and 878.

Details

Redox score ?

PDB code

Structure name

partial dimer complex of papp-a and its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

713

Residue number B

878

Peptide name

Pappalysin-1

Ligandability

Cysteine 713 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 878 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1192 and 1205 (1112 and 1125 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

cryo-em structure of substrate unbound papp-a

Structure deposition date

2022-06-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1192

Residue number B

1205

Peptide name

Pappalysin-1

Ligandability

Cysteine 1192 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1205 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1242 and 1280 (1162 and 1200 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1242

Residue number B

1280

Peptide name

Pappalysin-1

Ligandability

Cysteine 1242 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1280 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 999 and 1011.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

999

Residue number B

1011

Peptide name

Pappalysin-1

Ligandability

Cysteine 999 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1011 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1362 and 1373 (1282 and 1293 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1362

Residue number B

1373

Peptide name

Pappalysin-1

Ligandability

Cysteine 1362 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1373 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1377 and 1410 (1297 and 1330 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1377

Residue number B

1410

Peptide name

Pappalysin-1

Ligandability

Cysteine 1377 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1410 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1428 and 1438.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1428

Residue number B

1438

Peptide name

Pappalysin-1

Ligandability

Cysteine 1428 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1438 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1300 and 1310.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1300

Residue number B

1310

Peptide name

Pappalysin-1

Ligandability

Cysteine 1300 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1310 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 710 and 881.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

710

Residue number B

881

Peptide name

Pappalysin-1

Ligandability

Cysteine 710 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 881 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 414 and 428.

Details

Redox score ?

PDB code

Structure name

partial dimer complex of papp-a and its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

414

Residue number B

428

Peptide name

Pappalysin-1

Ligandability

Cysteine 414 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 428 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1285 and 1329 (1205 and 1249 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1285

Residue number B

1329

Peptide name

Pappalysin-1

Ligandability

Cysteine 1285 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1329 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1478 and 1539.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1478

Residue number B

1539

Peptide name

Pappalysin-1

Ligandability

Cysteine 1478 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1539 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1314 and 1342.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1314

Residue number B

1342

Peptide name

Pappalysin-1

Ligandability

Cysteine 1314 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1342 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1227 and 1238.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1227

Residue number B

1238

Peptide name

Pappalysin-1

Ligandability

Cysteine 1227 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1238 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1051 and 1139 (971 and 1059 respectively in this structure).

Details

Redox score ?

PDB code

7ufg

Structure name

cryo-em structure of papp-a in complex with igfbp5

Structure deposition date

2022-03-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1051

Residue number B

1139

Peptide name

Pappalysin-1

Ligandability

Cysteine 1051 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1139 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 983 and 990 (903 and 910 respectively in this structure).

Details

Redox score ?

PDB code

7ufg

Structure name

cryo-em structure of papp-a in complex with igfbp5

Structure deposition date

2022-03-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

983

Residue number B

990

Peptide name

Pappalysin-1

Ligandability

Cysteine 983 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 990 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1036 and 1070 (956 and 990 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

cryo-em structure of substrate unbound papp-a

Structure deposition date

2022-06-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1036

Residue number B

1070

Peptide name

Pappalysin-1

Ligandability

Cysteine 1036 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1070 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 457 and 473.

Details

Redox score ?

PDB code

Structure name

partial dimer complex of papp-a and its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

457

Residue number B

473

Peptide name

Pappalysin-1

Ligandability

Cysteine 457 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 473 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1506 and 1554 (1426 and 1474 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1506

Residue number B

1554

Peptide name

Pappalysin-1

Ligandability

Cysteine 1506 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1554 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1558 and 1576 (1478 and 1496 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1558

Residue number B

1576

Peptide name

Pappalysin-1

Ligandability

Cysteine 1558 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1576 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 775 and 781 (695 and 701 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

775

Residue number B

781

Peptide name

Pappalysin-1

Ligandability

Cysteine 775 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 781 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 1346 and 1399.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

1346

Residue number B

1399

Peptide name

Pappalysin-1

Ligandability

Cysteine 1346 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 1399 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 327 and 587.

Details

Redox score ?

PDB code

Structure name

partial dimer complex of papp-a and its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

327

Residue number B

587

Peptide name

Pappalysin-1

Ligandability

Cysteine 327 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 587 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 753 and 835 (673 and 755 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

cryo-em structure of substrate unbound papp-a

Structure deposition date

2022-06-08

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

753

Residue number B

835

Peptide name

Pappalysin-1

Ligandability

Cysteine 753 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 835 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 612 and 643.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

612

Residue number B

643

Peptide name

Pappalysin-1

Ligandability

Cysteine 612 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 643 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 474 and 485 (394 and 405 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

474

Residue number B

485

Peptide name

Pappalysin-1

Ligandability

Cysteine 474 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 485 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 144 and 235 (64 and 155 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

144

Residue number B

235

Peptide name

Pappalysin-1

Ligandability

Cysteine 144 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 235 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 332 and 657 (252 and 577 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

332

Residue number B

657

Peptide name

Pappalysin-1

Ligandability

Cysteine 332 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 657 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 947 and 975.

Details

Redox score ?

PDB code

Structure name

partial dimer complex of papp-a and its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

947

Residue number B

975

Peptide name

Pappalysin-1

Ligandability

Cysteine 947 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 975 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 583 and 622 (503 and 542 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

583

Residue number B

622

Peptide name

Pappalysin-1

Ligandability

Cysteine 583 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 622 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 960 and 971.

Details

Redox score ?

PDB code

Structure name

papp-a dimer in complex with its inhibitor stc2

Structure deposition date

2022-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

960

Residue number B

971

Peptide name

Pappalysin-1

Ligandability

Cysteine 960 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 971 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Pappalysin-1 between cysteines 424 and 440 (344 and 360 respectively in this structure).

Details

Redox score ?

PDB code

Structure name

structure of 2:2 papp-a

Structure deposition date

2022-11-14

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

424

Residue number B

440

Peptide name

Pappalysin-1

Ligandability

Cysteine 424 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.

Cysteine 440 of Pappalysin-1

Not ligandable in the dataset of Vinogradova et al.