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Crystal structure of the pH domain of skap-hom

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

PDB: 1U5G
Type: protein
Length: 466 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Src-associated adaptor protein
UniProt: Q8BK74
Pockets: 6 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Src-associated adaptor protein	protein	115	17% helix, 36% strand	Q8BK74
B, C	Src-associated adaptor protein	protein	118	22% helix, 35% strand	Q8BK74

Pockets

6 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	191	0.46	0.74	30	empty
2	113	0.43	0.77	17	empty
3	111	0.41	0.77	23	empty
4	81	0.36	0.76	22	empty
5	52	0.31	0.77	14	empty

Interfaces

3 interfaces between chains.

A–D · 767 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 365 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 142 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1U5G · Crystal Structure of the PH Domain of SKAP-Hom · 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 Q8BK74
Elsewhere: RCSB PDB 1U5G · PDBe 1U5G · UniProt Q8BK74

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