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Structure of the TIM14-TIM16 complex of the mitochondrial protein import motor

Analyse Structure of the TIM14-TIM16 complex of the mitochondrial protein import motor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GUZ
Type: protein
Length: 1,088 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitochondrial import inner membrane translocase subunit TIM14; Mitochondrial import inner…
UniProt: Q07914, P42949
Pockets: 16 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, G, I, K, M, O	Mitochondrial import inner membrane translocase subunit TIM14	protein	71	59% helix, 0% strand	Q07914
B, D, F, H, J, L, N, P	Mitochondrial import inner membrane translocase subunit TIM16	protein	65	75% helix, 0% strand	P42949

Ligands and binding sites

FLC · Citrate anion · additive · 4 copies · chains F, O, A, H, J, L

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

Pockets

16 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	934	0.80	0.82	63	empty
2	382	0.68	0.81	34	empty
3	515	0.65	0.77	47	empty
4	376	0.62	0.78	42	empty
5	140	0.49	0.78	32	empty

Interfaces

43 interfaces between chains.

E–F · 1119 Å² buried · 20 hydrogen bonds · protein-protein
K–L · 1114 Å² buried · 19 hydrogen bonds · protein-protein
I–J · 1106 Å² buried · 19 hydrogen bonds · protein-protein
G–H · 1091 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1078 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2GUZ · Structure of the Tim14-Tim16 complex of the mitochondrial protein import motor · the same entry in another collection · chain P against P, 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 Q07914
Every structure of UniProt P42949
Elsewhere: RCSB PDB 2GUZ · PDBe 2GUZ · UniProt Q07914 · UniProt P42949

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