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201PHI2-1 chimallin C1 localized reconstruction

Analyse 201PHI2-1 chimallin C1 localized reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7SQS
Type
protein
Length
560 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chimallin
UniProt
B3FIW8
Pockets
7 · best druggability 0.82

Structure

electron microscopy · 5 distinct chains · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChimallinprotein50835% helix, 24% strandB3FIW8
EChimallinprotein1443% helix, 0% strandB3FIW8
DChimallinprotein60% helix, 0% strandB3FIW8
CChimallinprotein100% helix, 0% strandB3FIW8
BChimallinprotein2214% helix, 0% strandB3FIW8

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19910.820.8495empty
25900.810.8660empty
3670.710.9717empty
41610.550.8129empty
51470.460.7721empty

Interfaces

4 interfaces between chains.

  • A–B · 1249 Ų buried · 10 hydrogen bonds · protein-protein
  • A–E · 761 Ų buried · 13 hydrogen bonds · protein-protein
  • A–C · 643 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 398 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 7SQS · 201phi2-1 Chimallin C1 localized reconstruction · the same entry in another collection · chain A against A, TM-score 1.00

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