Research workbench

Mouse mitochondrial complex I in the active state

Analyse Mouse mitochondrial complex I in the active state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G2J
Type: protein
Length: 8,164 residues
Chains: 45
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P03899, Q9DC70, Q9DCT2, Q91WD5, Q9D6J6, Q91YT0, Q91VD9, P03888, Q8K3J1, P03925, P03903, P03921, P03911, P03893, Q99LC3, Q9DC69, Q9CXZ1, P52503, Q9CQ75, Q9CR21, Q9CPP6, Q9CQZ5, Q9DCJ5, G5E814, Q9ERS2, O35683, Q9CQ91, Q9CQY9, Q9CQ54, Q99LY9, P0DN34, O09111, Q9CQH3, Q3UIU2, Q9CPU2, Q9CQZ6, Q9D6J5, Q9CQC7, Q9CQJ8, Q9CR61, Q9DCS9, Q7TMF3, Q9Z1P6, Q8BK30
Ligands: 3PE, SF4, PC1, CDL, FES, EHZ, FMN, ADP, NDP, ZN

Structure

electron microscopy · 45 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	115	—	P03899
B	—	protein	155	—	Q9DC70
C	—	protein	206	—	Q9DCT2
D	—	protein	430	—	Q91WD5
E	—	protein	212	—	Q9D6J6
F	—	protein	428	—	Q91YT0
G	—	protein	688	—	Q91VD9
H	—	protein	318	—	P03888
I	—	protein	178	—	Q8K3J1
J	—	protein	171	—	P03925
K	—	protein	98	—	P03903
L	—	protein	606	—	P03921
M	—	protein	459	—	P03911
N	—	protein	344	—	P03893
O	—	protein	320	—	Q99LC3
P	—	protein	342	—	Q9DC69
Q	—	protein	125	—	Q9CXZ1
R	—	protein	95	—	P52503
S	—	protein	83	—	Q9CQ75
T	—	protein	75	—	Q9CR21
U	—	protein	88	—	Q9CR21
V	—	protein	112	—	Q9CPP6
W	—	protein	114	—	Q9CQZ5
X	—	protein	171	—	Q9DCJ5
Y	—	protein	140	—	G5E814
Z	—	protein	139	—	Q9ERS2
a	—	protein	67	—	O35683
b	—	protein	83	—	Q9CQ91
c	—	protein	47	—	Q9CQY9
d	—	protein	119	—	Q9CQ54
e	—	protein	104	—	Q99LY9
f	—	protein	51	—	P0DN34
g	—	protein	101	—	O09111
h	—	protein	137	—	Q9CQH3
i	—	protein	101	—	Q3UIU2
j	—	protein	60	—	Q9CPU2
k	—	protein	72	—	Q9CQZ6
l	—	protein	152	—	Q9D6J5
m	—	protein	124	—	Q9CQC7
n	—	protein	176	—	Q9CQJ8
o	—	protein	105	—	Q9CR61
p	—	protein	170	—	Q9DCS9
q	—	protein	144	—	Q7TMF3
r	—	protein	99	—	Q9Z1P6
s	—	protein	40	—	Q8BK30

Ligands and binding sites

3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 12 copies · chains J, K, A, H, Z, a, D, I, b, L, l, h, i, M, N, Y, g, f, O, d
SF4 · Iron/sulfur cluster · ligand · 6 copies · chains B, D, F, G, I
PC1 · 1,2-diacyl-sn-glycero-3-phosphocholine · ligand · 4 copies · chains H, J, P, I, Z, r, B, q, A
CDL · Cardiolipin · ligand · 4 copies · chains H, a, q, r, L, M, g, h, i, p, N, X, d, f
FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains E, F, G
EHZ · ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (3~{S})-3-oxidanyltetradecanethioate · ligand · 2 copies · chains T, W, L, U, n
FMN · Flavin mononucleotide · ligand · chains F
ADP · Adenosine-5'-diphosphate · ligand · chains O
NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains B, P
ZN · Zinc ion · metal · chains R

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

Compared structures

6G2J · Mouse mitochondrial complex I in the active state · the same entry in another collection · chain I against I, 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 P03899
Every structure of UniProt Q9DC70
Every structure of UniProt Q9DCT2
Every structure of UniProt Q91WD5
Every structure of UniProt Q9D6J6
Every structure of UniProt Q91YT0
Every structure of UniProt Q91VD9
Every structure of UniProt P03888
Every structure of UniProt Q8K3J1
Every structure of UniProt P03925
Every structure of UniProt P03903
Every structure of UniProt P03921
Every structure of UniProt P03911
Every structure of UniProt P03893
Every structure of UniProt Q99LC3
Every structure of UniProt Q9DC69
Every structure of UniProt Q9CXZ1
Every structure of UniProt P52503
Every structure of UniProt Q9CQ75
Every structure of UniProt Q9CR21
Every structure of UniProt Q9CPP6
Every structure of UniProt Q9CQZ5
Every structure of UniProt Q9DCJ5
Every structure of UniProt G5E814
Every structure of UniProt Q9ERS2
Every structure of UniProt O35683
Every structure of UniProt Q9CQ91
Every structure of UniProt Q9CQY9
Every structure of UniProt Q9CQ54
Every structure of UniProt Q99LY9
Every structure of UniProt P0DN34
Every structure of UniProt O09111
Every structure of UniProt Q9CQH3
Every structure of UniProt Q3UIU2
Every structure of UniProt Q9CPU2
Every structure of UniProt Q9CQZ6
Every structure of UniProt Q9D6J5
Every structure of UniProt Q9CQC7
Every structure of UniProt Q9CQJ8
Every structure of UniProt Q9CR61
Every structure of UniProt Q9DCS9
Every structure of UniProt Q7TMF3
Every structure of UniProt Q9Z1P6
Every structure of UniProt Q8BK30
Elsewhere: RCSB PDB 6G2J · PDBe 6G2J · UniProt P03899 · UniProt Q9DC70 · UniProt Q9DCT2 · UniProt Q91WD5 · UniProt Q9D6J6 · UniProt Q91YT0 · UniProt Q91VD9 · UniProt P03888 · UniProt Q8K3J1 · UniProt P03925 · UniProt P03903 · UniProt P03921 · UniProt P03911 · UniProt P03893 · UniProt Q99LC3 · UniProt Q9DC69 · UniProt Q9CXZ1 · UniProt P52503 · UniProt Q9CQ75 · UniProt Q9CR21 · UniProt Q9CPP6 · UniProt Q9CQZ5 · UniProt Q9DCJ5 · UniProt G5E814 · UniProt Q9ERS2 · UniProt O35683 · UniProt Q9CQ91 · UniProt Q9CQY9 · UniProt Q9CQ54 · UniProt Q99LY9 · UniProt P0DN34 · UniProt O09111 · UniProt Q9CQH3 · UniProt Q3UIU2 · UniProt Q9CPU2 · UniProt Q9CQZ6 · UniProt Q9D6J5 · UniProt Q9CQC7 · UniProt Q9CQJ8 · UniProt Q9CR61 · UniProt Q9DCS9 · UniProt Q7TMF3 · UniProt Q9Z1P6 · UniProt Q8BK30

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