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Structure of pro-activin a precursor at 2.3 a resolution

Analyse Structure of pro-activin a precursor at 2.3 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HLY
Type: protein
Length: 299 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inhibin beta a chain
UniProt: P08476
Ligands: CL
Pockets: 3 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inhibin beta a chain	protein	299	19% helix, 42% strand	P08476

Ligands and binding sites

CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.39	0.76	21	empty
2	90	0.38	0.76	17	empty
3	59	0.28	0.73	14	empty

Modifications

Observed in the structure: 8 modified, 5 disulfide (engineered, disulfide).

Compared structures

5HLY · Structure of Pro-Activin A Precursor at 2.3 A Resolution · the same entry in another collection · chain A against A, 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 5HLY · PDBe 5HLY · UniProt P08476

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