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Structure of mutant rip from barley seeds

Analyse Structure of mutant rip from barley seeds in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4FB9
Type
protein
Length
1,114 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein synthesis inhibitor I
EC
3.2.2.22
UniProt
P22244
Pockets
19 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein synthesis inhibitor I (EC 3.2.2.22)protein27839% helix, 16% strandP22244
C, DProtein synthesis inhibitor I (EC 3.2.2.22)protein27939% helix, 15% strandP22244

Pockets

19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110580.740.7773empty
29990.730.7665empty
31950.560.8034empty
41720.510.7832empty
51930.510.7732empty

Interfaces

5 interfaces between chains.

  • A–B · 838 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 812 Ų buried · 16 hydrogen bonds · protein-protein
  • A–D · 450 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 447 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 40 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

  • 4FB9 · Structure of mutant RIP from barley seeds · the same entry in another collection · chain A against A, TM-score 1.00
  • P22244 · AlphaFold monomer V2.0 prediction for protein synthesis inhibitor I (P22244) · a predicted model of the same protein · chain A against A, TM-score 0.99

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