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MolNFT v1 · #47785 · protein

Fitted structure of EEF2 in the 80S:EEF2:GDPNP cryo-EM reconstruction

2P8W · Elongation factor 2: “Fitted structure of EEF2 in the 80S:EEF2:GDPNP cryo-EM reconstruction”. Electron microscopy, 1 ligand (GNP), 12 pockets (best druggability 0.78). MolNFT v1 #47785 on GenesisL1: 3D structure, binding sites and…

PDB
2P8W
Type
protein
Length
849 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor 2; Elongation factor tu-B
UniProt
P32324, P60339
Ligands
GNP
Pockets
12 · best druggability 0.78

Structure

electron microscopy · 2 distinct chains · 36% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
TElongation factor 2protein81437% helix, 23% strandP32324
SElongation factor tu-Bprotein3526% helix, 9% strandP60339

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains T, S

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

Pockets

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11560.780.9428empty
29400.760.7986empty
32700.720.8542empty
47170.710.7766empty
51510.660.8743GNP

Interfaces

1 interface between chains.

  • T–S · 1522 Ų buried · 74 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 covalent, 1 isopeptide (covalent ligand, isopeptide).

Compared structures

  • 2P8W · Fitted structure of eEF2 in the 80S:eEF2:GDPNP cryo-EM reconstruction · the same entry in another collection · chain T against T, TM-score 1.00
  • P60339 · AlphaFold monomer V2.0 prediction for elongation factor tu-B (P60339) · a predicted model of the same protein · chain S against A, TM-score 0.91
  • P32324 · AlphaFold monomer V2.0 prediction for elongation factor 2 (P32324) · a predicted model of the same protein · chain T against A, TM-score 0.67

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