MolNFT v1 · #158806 · protein

Human mcu-emre complex, dimer of channel

6O58 · Calcium uniporter protein, mitochondrial: “Human mcu-emre complex, dimer of channel”. Electron microscopy, 1 ligand (CA), 20 pockets (best druggability 0.75). MolNFT v1 #158806 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6O58
Type: protein
Length: 2,512 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calcium uniporter protein, mitochondrial; Essential mcu regulator, mitochondrial
UniProt: Q8NE86, Q9H4I9
Ligands: CA
Pockets: 20 · best druggability 0.75

Structure

electron microscopy · 6 distinct chains · 60% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
K, C	Calcium uniporter protein, mitochondrial	protein	268	60% helix, 12% strand	Q8NE86
L, N, J, D, B, F	Essential mcu regulator, mitochondrial	protein	49	55% helix, 0% strand	Q9H4I9
O, G	Calcium uniporter protein, mitochondrial	protein	250	62% helix, 11% strand	Q8NE86
P, H	Essential mcu regulator, mitochondrial	protein	48	60% helix, 4% strand	Q9H4I9
M, E	Calcium uniporter protein, mitochondrial	protein	270	58% helix, 11% strand	Q8NE86
I, A	Calcium uniporter protein, mitochondrial	protein	273	60% helix, 12% strand	Q8NE86

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains K, O, M, I, G, C, A, E

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.75	0.96	21	empty
2	140	0.75	0.93	35	empty
3	1179	0.74	0.77	98	empty
4	876	0.73	0.78	59	empty
5	586	0.73	0.80	50	empty

Interfaces

35 interfaces between chains.

M–I · 2401 Å² buried · 11 hydrogen bonds · protein-protein
A–E · 2322 Å² buried · 12 hydrogen bonds · protein-protein
C–A · 2138 Å² buried · 16 hydrogen bonds · protein-protein
K–I · 2137 Å² buried · 19 hydrogen bonds · protein-protein
K–O · 1730 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6O58 · Human MCU-EMRE complex, dimer of channel · the same entry in another collection · chain C against C, 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 Q8NE86
Every structure of UniProt Q9H4I9
Elsewhere: RCSB PDB 6O58 · PDBe 6O58 · UniProt Q8NE86 · UniProt Q9H4I9

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