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Cryo-EM structure of pre-dephosphorylation complex of phosphorylated EIF2ALPHA with trapped holophosphatase (PP1A_D64A/PPP1R15A/G- ACTIN/DNASE I)

Analyse Cryo-EM structure of pre-dephosphorylation complex of phosphorylated EIF2ALPHA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NZM
Type
protein
Length
1,157 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Eukaryotic translation initiation factor 2 subunit 1; SERINE/THREONINE-protein…
EC
3.1.3.16, 3.1.21.1
UniProt
P05198, P62139, P68135, P00639, O75807
Ligands
ATP, NAG, MN
Pockets
13 · best druggability 0.75

Structure

electron microscopy · 5 distinct chains · 39% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
EEukaryotic translation initiation factor 2 subunit 1protein17844% helix, 19% strandP05198
BSERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit (EC 3.1.3.16)protein29334% helix, 17% strandP62139
AActin, alpha skeletal muscle, intermediate formprotein37044% helix, 21% strandP68135
DDeoxyribonuclease-1 (EC 3.1.21.1)protein25730% helix, 26% strandP00639
CProtein phosphatase 1 regulatory subunit 15A, MALTOSE/MALTODEXTRIN-binding periplasmic proteinprotein5956% helix, 7% strandO75807

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains D
  • MN · Manganese (II) ion · metal · chains E, B

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

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14700.750.8450ATP
21780.670.8730empty
32520.670.8440empty
4530.670.9516empty
55750.650.7658empty

Interfaces

8 interfaces between chains.

  • B–C · 1224 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 1003 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 951 Ų buried · 7 hydrogen bonds · protein-protein
  • E–B · 622 Ų buried · 17 hydrogen bonds · protein-protein
  • E–C · 525 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, phosphorylation).

Compared structures

  • 7NZM · Cryo-EM structure of pre-dephosphorylation complex of phosphorylated eIF2alpha with… · the same entry in another collection · chain C against C, TM-score 1.00
  • P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • P00639 · AlphaFold monomer V2.0 prediction for deoxyribonuclease-1 (P00639) · a predicted model of the same protein · chain D against A, TM-score 0.97
  • P62139 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PP1-alpha… · a predicted model of the same protein · chain B against A, TM-score 0.96
  • P05198 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 2 subunit… · a predicted model of the same protein · chain E against A, TM-score 0.91
  • O75807 · AlphaFold monomer V2.0 prediction for protein phosphatase 1 regulatory subunit 15A… · a predicted model of the same protein · chain C against A, TM-score 0.59

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