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Crystal structure of the AP1H peptide homodimer.

Analyse Crystal structure of the AP1H peptide homodimer. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DXS
Type: protein
Length: 183 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AP1H protein
Ligands: SO4
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 3 distinct chains · 22% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	AP1H protein	protein	46	22% helix, 39% strand	—
B, D	AP1H protein	protein	44	23% helix, 41% strand	—
C	AP1H protein	protein	49	20% helix, 35% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 9 copies · chains A, B, D, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.38	0.79	18	empty

Interfaces

6 interfaces between chains.

A–B · 2360 Å² buried · 53 hydrogen bonds · protein-protein
C–D · 2310 Å² buried · 52 hydrogen bonds · protein-protein
B–C · 220 Å² buried · 1 hydrogen bond · protein-protein
A–D · 214 Å² buried · 3 hydrogen bonds · protein-protein
B–D · 144 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7DXS · Crystal structure of the ap1h peptide homodimer. · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 7DXS · PDBe 7DXS

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