Research workbench

S4AFL3ARG515 mutant

Analyse S4AFL3ARG515 mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G88
Type: protein
Length: 699 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SMAD4
UniProt: Q13485
Pockets: 10 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 25% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SMAD4	protein	221	23% helix, 29% strand	Q13485
B	SMAD4	protein	242	26% helix, 27% strand	Q13485
C	SMAD4	protein	236	24% helix, 28% strand	Q13485

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1196	0.86	0.87	107	empty
2	254	0.63	0.81	41	empty
3	177	0.58	0.82	35	empty
4	77	0.45	0.81	21	empty
5	136	0.45	0.77	27	empty

Interfaces

3 interfaces between chains.

A–B · 1007 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 980 Å² buried · 14 hydrogen bonds · protein-protein
A–C · 847 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1G88 · S4AFL3ARG515 mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q13485 · AlphaFold monomer V2.0 prediction for mothers against decapentaplegic homolog 4 (Q13485) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q13485
Elsewhere: RCSB PDB 1G88 · PDBe 1G88 · UniProt Q13485

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