Research workbench

Semet substituted stid O-mt residues 976-1266

Analyse Semet substituted stid O-mt residues 976-1266 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ECU
Type: protein
Length: 554 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stid protein
UniProt: Q8RJY3
Ligands: SAH
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Stid protein	protein	275	45% helix, 21% strand	Q8RJY3
B	Stid protein	protein	279	46% helix, 20% strand	Q8RJY3

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B

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

Pockets

6 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	403	0.73	0.84	39	SAH
2	424	0.64	0.78	49	SAH
3	178	0.52	0.78	24	empty
4	95	0.40	0.77	21	empty
5	84	0.39	0.77	11	empty

Interfaces

1 interface between chains.

A–B · 1250 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

6ECU · SeMet substituted StiD O-MT residues 976-1266 · 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 Q8RJY3
Elsewhere: RCSB PDB 6ECU · PDBe 6ECU · UniProt Q8RJY3

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