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High resolution crystal structure of C3PO

Analyse High resolution crystal structure of C3PO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AXJ
Type
protein
Length
465 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GM27569P; Translin associated factor X, isoform B
UniProt
Q7JVK6, Q8INE1
Pockets
5 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGM27569Pprotein22578% helix, 1% strandQ7JVK6
BTranslin associated factor X, isoform Bprotein24075% helix, 3% strandQ8INE1

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12500.570.7927empty
22960.570.7733empty
31840.520.7920empty
4630.360.7912empty
5620.330.7716empty

Interfaces

1 interface between chains.

  • A–B · 2153 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 3AXJ · High resolution crystal structure of C3PO · the same entry in another collection · chain A against A, TM-score 1.00

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