Bone morphogenetic protein 2

Structure name

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

465

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between two units of Bone morphogenetic protein 2 at cysteines 360 and 360 (78 and 78 respectively in this structure).

Details

Redox score ?

PDB code

2qjb

Structure name

crystal structure analysis of bmp-2 in complex with bmpr-ia variant ia/ib

Structure deposition date

2007-07-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Bone morphogenetic protein 2

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

360

Ligandability

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 329 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (47 and 84 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

329

Peptide B residue number

465

Ligandability

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 466 of Growth/differentiation factor 5 (78 and 85 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

466

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 466 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 433 of Growth/differentiation factor 5 (78 and 52 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

433

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 433 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 361 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (79 and 84 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

361

Peptide B residue number

465

Ligandability

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 400 of Growth/differentiation factor 5 (78 and 19 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

400

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 400 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 296 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (14 and 84 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

296

Peptide B residue number

465

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 429 of Growth/differentiation factor 5 (78 and 48 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

429

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 429 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 325 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (43 and 84 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

325

Peptide B residue number

465

Ligandability

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 395 of Bone morphogenetic protein 2 and cysteine 465 of Growth/differentiation factor 5 (113 and 84 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

395

Peptide B residue number

465

Ligandability

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 465 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form between cysteine 360 of Bone morphogenetic protein 2 and cysteine 500 of Growth/differentiation factor 5 (78 and 119 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

Bone morphogenetic protein 2

Peptide B name

Growth/differentiation factor 5

Peptide A accession

Peptide B accession

Peptide A residue number

360

Peptide B residue number

500

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 500 of Growth/differentiation factor 5

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 361 (14 and 79 respectively in this structure).

Details

Redox score ?

PDB code

3bmp

Structure name

human bone morphogenetic protein-2 (bmp-2)

Structure deposition date

1999-03-12

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

361

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 329 and 395.

Details

Redox score ?

PDB code

Structure name

crystal structure of the human rgmb-bmp2 complex, crystal form 2

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

329

Residue number B

395

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 325 and 393 (43 and 111 respectively in this structure).

Details

Redox score ?

PDB code

1rew

Structure name

structural refinement of the complex of bone morphogenetic protein 2 and its type ia receptor

Structure deposition date

2003-11-07

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

325

Residue number B

393

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 393 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 329.

Details

Redox score ?

PDB code

4ui1

Structure name

crystal structure of the human rgmc-bmp2 complex

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

329

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 395 (14 and 113 respectively in this structure).

Details

Redox score ?

PDB code

3bmp

Structure name

human bone morphogenetic protein-2 (bmp-2)

Structure deposition date

1999-03-12

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

395

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 325 and 361 (43 and 80 respectively in this structure).

Details

Redox score ?

PDB code

4n1d

Structure name

nodal/bmp2 chimera nb250

Structure deposition date

2013-10-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

325

Residue number B

361

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 361 and 393 (80 and 112 respectively in this structure).

Details

Redox score ?

PDB code

4n1d

Structure name

nodal/bmp2 chimera nb250

Structure deposition date

2013-10-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

361

Residue number B

393

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 393 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 393.

Details

Redox score ?

PDB code

Structure name

crystal structure of the human rgmb-bmp2 complex, crystal form 2

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

393

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 393 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 361 and 395 (80 and 114 respectively in this structure).

Details

Redox score ?

PDB code

4n1d

Structure name

nodal/bmp2 chimera nb250

Structure deposition date

2013-10-04

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

361

Residue number B

395

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 329 and 361.

Details

Redox score ?

PDB code

Structure name

crystal structure of the human rgmb-bmp2 complex, crystal form 2

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

329

Residue number B

361

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 325 (14 and 43 respectively in this structure).

Details

Redox score ?

PDB code

2qj9

Structure name

crystal structure analysis of bmp-2 in complex with bmpr-ia variant b1

Structure deposition date

2007-07-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

325

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 329 and 360. 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 the human rgmb-bmp2 complex, crystal form 2

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

329

Residue number B

360

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 296 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4uhy

Structure name

crystal structure of the human rgma-bmp2 complex

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

296

Residue number B

360

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 296 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 393 and 395 (111 and 113 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

2h64

Structure name

crystal structure of a ternary ligand-receptor complex of bmp-2

Structure deposition date

2006-05-30

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

393

Residue number B

395

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 393 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 325 and 329 (43 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

1rew

Structure name

structural refinement of the complex of bone morphogenetic protein 2 and its type ia receptor

Structure deposition date

2003-11-07

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

325

Residue number B

329

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 360 and 361 (78 and 79 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

360

Residue number B

361

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 361 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 329 and 393 (47 and 111 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

2goo

Structure name

ternary complex of bmp-2 bound to bmpr-ia-ecd and actrii-ecd

Structure deposition date

2006-04-13

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

329

Residue number B

393

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 329 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 393 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 360 and 395 (78 and 113 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

bmp2/gdf5 heterodimer

Structure deposition date

2022-08-17

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

360

Residue number B

395

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 395 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

A redox-regulated disulphide may form within Bone morphogenetic protein 2 between cysteines 325 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4uhy

Structure name

crystal structure of the human rgma-bmp2 complex

Structure deposition date

2015-03-27

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

325

Residue number B

360

Peptide name

Bone morphogenetic protein 2

Ligandability

Cysteine 325 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.

Cysteine 360 of Bone morphogenetic protein 2

Not ligandable in the dataset of Vinogradova et al.