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MolNFT v1 · #149866 · protein

Cryo-EM structure of respiratory complex I from yarrowia lipolytica

6GCS · 75-kda protein (nuam): “Cryo-EM structure of respiratory complex I from yarrowia lipolytica”. Electron microscopy, 8 ligands (SF4, 3PE, FES), 20 pockets (best druggability 0.90). MolNFT v1 #149866 on GenesisL1: 3D structure, binding…

PDB
6GCS
Type
protein
Length
7,515 residues
Chains
42
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
75-kda protein (nuam); 51-kda protein (nubm); 49-kda protein (nucm); Nimm subunit; Nuem…
EC
1.6.99.3, 1.6.5.3
UniProt
Q9UUU3, Q9UUU2, Q9UUU1, A0A1D8NC63, Q6C7X4, Q6C4W9, Q9UUU0, Q9UUT9, Q9UUT8, Q6C674, Q9UUT7, Q9B6D4, A0A1H6Q8Z5, A0A1H6PXT9, A0A1D8N3C8, A0A1D8NG21, A0A1D8NDL1, Q6CGB4, A0A1H6PPE5, A0A1D8NKB4, A0A1D8N7X0, B5FVE5, A0A1D8N596, A0A1H6PJS3, A0A1D8NJR0, Q6CG53, Q6ZY24, Q9B6E8, Q9B6C8, Q9B6C7, Q9B6D6, Q9B6D3, Q9B6E9, A0A1H6PKH9, A0A1D8NNZ0
Ligands
SF4, 3PE, FES, FMN, NDP, ZMP, CDL, ZN
Pockets
20 · best druggability 0.90

Structure

electron microscopy · 42 distinct chains · 45% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A75-kda protein (nuam) (EC 1.6.99.3)protein68928% helix, 13% strandQ9UUU3
B51-kda protein (nubm) (EC 1.6.5.3, 1.6.99.3)protein44340% helix, 12% strandQ9UUU2
C49-kda protein (nucm) (EC 1.6.99.3)protein41642% helix, 11% strandQ9UUU1
DNimm subunitprotein8051% helix, 6% strandA0A1D8NC63
ENuem subunitprotein31830% helix, 11% strandQ6C7X4
FNufm subunitprotein11951% helix, 0% strandQ6C4W9
G30-kda protein (nugm) (EC 1.6.99.3)protein23215% helix, 17% strandQ9UUU0
H24-kda subunit (nuhm) (EC 1.6.99.3)protein18537% helix, 10% strandQ9UUT9
ITyky subunit (nuim) (EC 1.6.99.3)protein18026% helix, 12% strandQ9UUT8
JNujm subunitprotein14051% helix, 0% strandQ6C674
KPsst subunit (nukm) (EC 1.6.99.3)protein16934% helix, 11% strandQ9UUT7
LND4L subunit (nulm) (EC 1.6.5.3)protein8672% helix, 0% strandQ9B6D4
MNumm subunitprotein1056% helix, 13% strandA0A1H6Q8Z5
OACPM1 subunitprotein7751% helix, 3% strandA0A1H6PXT9
PNB4M subunitprotein11655% helix, 0% strandA0A1D8N3C8
QACPM2 subunitprotein8549% helix, 2% strandA0A1D8NG21
RNI2M subunitprotein10250% helix, 0% strandA0A1D8NDL1
SNesm subunit (EC 1.6.5.3)protein15955% helix, 0% strand—
UNupm subunitprotein15853% helix, 2% strandQ6CGB4
WNB6M subunitprotein11855% helix, 0% strandA0A1H6PPE5
XNuxm subunitprotein11739% helix, 0% strandA0A1D8NKB4
YNuym subunitprotein11516% helix, 14% strandA0A1D8N7X0
ZNuzm subunit (EC 1.6.5.3)protein13718% helix, 4% strand—
aNiam subunit (EC 1.6.5.3)protein10013% helix, 0% strand—
bNebm subunit (EC 1.6.5.3)protein6470% helix, 0% strand—
cNB2M subunitprotein4250% helix, 0% strandB5FVE5
dNidm subunitprotein8955% helix, 0% strandA0A1D8N596
eNuum subunit (EC 1.6.5.3)protein4547% helix, 0% strand—
fNI8M subunitprotein8026% helix, 25% strandA0A1H6PJS3
gNI9M subunitprotein6038% helix, 0% strandA0A1D8NJR0
hN7BM subunitprotein13015% helix, 5% strandQ6CG53
iUnknown subunit (EC 1.6.5.3)protein5360% helix, 0% strand—
jNB5M subunit (EC 1.6.99.3)protein7342% helix, 0% strandQ6ZY24
nNunm subunit (EC 1.6.5.3)protein9342% helix, 0% strand—
1ND1 subunit (NU1M) (EC 1.6.5.3)protein34065% helix, 0% strandQ9B6E8
2ND2 subunit (NU2M) (EC 1.6.5.3)protein45265% helix, 2% strandQ9B6C8
3ND3 subunit (NU3M) (EC 1.6.5.3)protein11058% helix, 0% strandQ9B6C7
4ND4 subunit (NU4M) (EC 1.6.5.3)protein47556% helix, 0% strandQ9B6D6
5ND5 subunit (NU5M) (EC 1.6.5.3)protein63961% helix, 2% strandQ9B6D3
6ND6 subunit (NU6M) (EC 1.6.5.3)protein18363% helix, 2% strandQ9B6E9
8NB8M subunitprotein8263% helix, 0% strandA0A1H6PKH9
9Nipm subunitprotein5958% helix, 0% strandA0A1D8NNZ0

Ligands and binding sites

  • SF4 · Iron/sulfur cluster · ligand · 6 copies · chains A, C, B, I, K
  • 3PE · 1,2-diacyl-sn-glycero-3-phosphoethanolamine · ligand · 3 copies · chains g, 1, 2, 3, C, I, W, b, 4
  • FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, H
  • FMN · Flavin mononucleotide · ligand · chains B
  • NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains E, K
  • ZMP · S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy) butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate · ligand · chains O, P
  • CDL · Cardiolipin · ligand · chains X, g, 2, 3, 6
  • ZN · Zinc ion · metal · chains M

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110840.900.92127NDP
211160.890.91107empty
311170.880.90117empty
49240.880.90132empty
58750.880.90146empty

Interfaces

174 interfaces between chains.

  • 1–3 · 2735 Ų buried · 6 hydrogen bonds · protein-protein
  • C–G · 2681 Ų buried · 19 hydrogen bonds · protein-protein
  • A–Y · 2484 Ų buried · 26 hydrogen bonds · protein-protein
  • L–6 · 2428 Ų buried · 4 hydrogen bonds · protein-protein
  • B–H · 2377 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

  • 6GCS · Cryo-EM structure of respiratory complex I from Yarrowia lipolytica · the same entry in another collection · chain K against K, TM-score 1.00

Analyse

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