Research workbench

Crystal structure of the C-src SH3 domain mutant V111L-N113S-T114S- Q128E at pH 7.0

Analyse Crystal structure of the C-src SH3 domain mutant V111L-N113S-T114S- Q128E at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A39
Type: protein
Length: 117 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene tyrosine-protein kinase src
EC: 2.7.10.2
UniProt: P00523
Ligands: SO4
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	58	5% helix, 43% strand	P00523
B	Proto-oncogene tyrosine-protein kinase src (EC 2.7.10.2)	protein	59	5% helix, 46% strand	P00523

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	122	0.51	0.80	18	SO4

Interfaces

1 interface between chains.

A–B · 383 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7A39 · Crystal structure of the c-Src SH3 domain mutant V111L-N113S-T114S-Q128E at pH 7.0 · 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 P00523
Elsewhere: RCSB PDB 7A39 · PDBe 7A39 · UniProt P00523

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