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Structure of pro-activin a complex at 2.85 a resolution

Analyse Structure of pro-activin a complex at 2.85 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HLZ
Type: protein
Length: 1,154 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inhibin beta a chain
UniProt: P08476
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 4 distinct chains · 13% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G	Inhibin beta a chain	protein	204	28% helix, 36% strand	P08476
B, F	Inhibin beta a chain	protein	86	5% helix, 57% strand	P08476
D	Inhibin beta a chain	protein	82	0% helix, 57% strand	P08476
H	Inhibin beta a chain	protein	84	0% helix, 51% strand	P08476

Pockets

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	521	0.78	0.86	70	empty
2	164	0.77	0.94	26	empty
3	560	0.72	0.80	72	empty
4	211	0.53	0.78	24	empty
5	255	0.51	0.75	34	empty

Interfaces

15 interfaces between chains.

A–C · 1553 Å² buried · 7 hydrogen bonds · protein-protein
E–G · 1551 Å² buried · 8 hydrogen bonds · protein-protein
H–G · 1527 Å² buried · 10 hydrogen bonds · protein-protein
F–E · 1455 Å² buried · 10 hydrogen bonds · protein-protein
D–C · 1449 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 disulfide (disulfide).

Compared structures

5HLZ · Structure of Pro-Activin A Complex at 2.85 A resolution · the same entry in another collection · chain G against G, TM-score 1.00
P08476 · AlphaFold monomer V2.0 prediction for inhibin beta a chain (P08476) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P08476
Elsewhere: RCSB PDB 5HLZ · PDBe 5HLZ · UniProt P08476

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