MolNFT v1 · #147434 · protein

Stid O-mt residues 956-1266

6ECW · Stid protein: “Stid O-mt residues 956-1266”. X-ray diffraction, 1 ligand (SAH), 6 pockets (best druggability 0.72). MolNFT v1 #147434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6ECW
Type: protein
Length: 561 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 0.72

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Stid protein	protein	281	46% helix, 21% strand	Q8RJY3
B	Stid protein	protein	280	46% helix, 21% 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	524	0.72	0.81	44	SAH
2	436	0.68	0.80	43	SAH
3	166	0.49	0.77	20	empty
4	179	0.49	0.77	28	empty
5	61	0.46	0.84	22	empty

Interfaces

1 interface between chains.

A–B · 1130 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

6ECW · StiD O-MT residues 956-1266 · 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 6ECW · PDBe 6ECW · UniProt Q8RJY3

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