GL1X · GenesisL1 explorer

MolNFT v1 · #187186 · protein

Cryoem structure of methylococcus capsulatus (bath) pmmo in a native lipid nanodisc at 2.34 ångström resolution

7S4K: “Cryoem structure of methylococcus capsulatus (bath) pmmo in a native lipid nanodisc at 2.34 ångström…”. Electron microscopy, 5 ligands (D10, PLC, P1O). MolNFT v1 #187186 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7S4K
Type
protein
Length
2,577 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
G1UBD1, Q603F1, Q607G3
Ligands
D10, PLC, P1O, HXG, CU

Structure

electron microscopy · 3 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A, E, I—protein382—G1UBD1
C, G, K—protein236—Q603F1
B, F, J—protein241—Q607G3

Ligands and binding sites

  • D10 · Decane · ligand · 18 copies · chains B, F, J
  • PLC · Diundecyl phosphatidyl choline · ligand · 18 copies · chains C, F, A, B, I, K, G, E, J
  • P1O · 1,2-didecanoyl-sn-glycero-3-phosphocholine · ligand · 12 copies · chains C, B, F, K, G, J
  • HXG · 1,2-dihexanoyl-sn-glycero-3-phosphocholine · ligand · 6 copies · chains C, B, G, F, K, J
  • CU · Copper (II) ion · metal · 9 copies · chains A, C, G, K, E, I

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

Compared structures

  • 7S4K · CryoEM structure of Methylococcus capsulatus (Bath) pMMO in a native lipid nanodisc at… · the same entry in another collection · chain J against J, TM-score 1.00
  • Q607G3 · AlphaFold monomer V2.0 prediction for particulate methane monooxygenase beta subunit… · a predicted model of the same protein · chain B against A, TM-score 0.99
  • G1UBD1 · AlphaFold monomer V2.0 prediction for particulate methane monooxygenase alpha subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.