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Sas-4 (dcpap) tcp domain in complex with a proline rich motif of ANA2 (dstil) of drosophila melanogaster

Analyse Sas-4 (dcpap) tcp domain in complex with a proline rich motif of ANA2 (dstil)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4BY2
Type
protein
Length
464 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anastral spindle 2, sas 4
UniProt
Q9XZ31, Q9VI72
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnastral spindle 2, sas 4protein1540% helix, 45% strandQ9XZ31, Q9VI72
BAnastral spindle 2, sas 4protein1550% helix, 44% strandQ9XZ31, Q9VI72
CAnastral spindle 2, sas 4protein1550% helix, 44% strandQ9XZ31, Q9VI72

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · chains B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13680.690.8136EDO
23760.630.7845empty
32540.520.7629empty

Interfaces

2 interfaces between chains.

  • B–C · 873 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 521 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 4BY2 · SAS-4 (dCPAP) TCP domain in complex with a Proline Rich Motif of Ana2 (dSTIL) of… · the same entry in another collection · chain A against A, TM-score 1.00

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