Research workbench

Crystal structure of the pH domain of SKAP55

Analyse Crystal structure of the pH domain of SKAP55 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U5D
Type: protein
Length: 430 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Src kinase-associated phosphoprotein of 55 kda
UniProt: O15268
Ligands: SO4
Pockets: 2 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Src kinase-associated phosphoprotein of 55 kda	protein	108	24% helix, 42% strand	O15268
B, C	Src kinase-associated phosphoprotein of 55 kda	protein	107	19% helix, 40% strand	O15268

Ligands and binding sites

SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D

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

Pockets

2 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	71	0.29	0.73	14	empty
2	59	0.29	0.74	14	SO4

Interfaces

1 interface between chains.

A–D · 78 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1U5D · Crystal Structure of the PH domain of SKAP55 · 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
Every structure of UniProt O15268
Elsewhere: RCSB PDB 1U5D · PDBe 1U5D · UniProt O15268

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.