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EPYC1(106-135) peptide-bound rubisco

Analyse EPYC1(106-135) peptide-bound rubisco in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JSX
Type
protein
Length
4,832 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase small…
EC
4.1.1.39
UniProt
A0A218N8A3, P08475, A0A2K3DA85
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 3 distinct chains · 39% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, K, M, ORibulose bisphosphate carboxylase large chain (EC 4.1.1.39)protein44443% helix, 18% strandA0A218N8A3
B, D, F, H, J, L, N, PRibulose bisphosphate carboxylase small chain 2, chloroplastic (EC 4.1.1.39)protein13826% helix, 22% strandP08475
q, r, s, t, u, v, w, xEPYC1protein2241% helix, 0% strandA0A2K3DA85

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110340.860.87122empty
210340.860.87128empty
310660.850.86123empty
410480.850.86125empty
510570.850.86126empty

Interfaces

64 interfaces between chains.

  • E–G · 3162 Ų buried · 65 hydrogen bonds · protein-protein
  • M–O · 3161 Ų buried · 65 hydrogen bonds · protein-protein
  • I–K · 3155 Ų buried · 65 hydrogen bonds · protein-protein
  • A–C · 3148 Ų buried · 67 hydrogen bonds · protein-protein
  • A–P · 1986 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 4 disulfide (methylation, disulfide).

Compared structures

  • 7JSX · EPYC1(106-135) peptide-bound Rubisco · the same entry in another collection · chain H against H, TM-score 1.00

Analyse

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