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Mitochondrial SAM complex - dimer 3 in detergent

Analyse Mitochondrial SAM complex - dimer 3 in detergent in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WUN
Type: protein
Length: 1,326 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SAM35; BAC_SURFACE_AG domain-containing protein
UniProt: G2QAT9, G2QFF9
Pockets: 14 · best druggability 0.76

Structure

electron microscopy · 2 distinct chains · 24% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	SAM35	protein	260	47% helix, 5% strand	G2QAT9
B, D	BAC_SURFACE_AG domain-containing protein	protein	403	9% helix, 24% strand	G2QFF9

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1005	0.76	0.78	95	empty
2	1035	0.75	0.77	96	empty
3	505	0.59	0.74	43	empty
4	96	0.58	0.87	25	empty
5	464	0.58	0.74	44	empty

Interfaces

3 interfaces between chains.

C–D · 1966 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1947 Å² buried · 12 hydrogen bonds · protein-protein
B–D · 528 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6WUN · Mitochondrial SAM complex - dimer 3 in detergent · 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 G2QAT9
Every structure of UniProt G2QFF9
Elsewhere: RCSB PDB 6WUN · PDBe 6WUN · UniProt G2QAT9 · UniProt G2QFF9

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