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Crystal structure of sacuvde

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

PDB
3TC3
Type
protein
Length
579 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
UV damage endonuclease
EC
3.-.-.-
UniProt
Q4J9T1
Ligands
MN
Pockets
9 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUV damage endonuclease (EC 3.-.-.-)protein28945% helix, 13% strandQ4J9T1
BUV damage endonuclease (EC 3.-.-.-)protein29044% helix, 13% strandQ4J9T1

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11940.470.7522empty
21970.440.7334empty
31640.420.7417empty
41340.390.7421empty
51040.340.7320empty

Interfaces

1 interface between chains.

  • A–B · 17 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3TC3 · Crystal Structure of SacUVDE · the same entry in another collection · chain A against A, TM-score 1.00

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