MolNFT v1 · #110069 · protein

C. glabrata SLX1 in complex with SLX4CCD.

4XLG · Structure-specific endonuclease subunit SLX4: “C. glabrata SLX1 in complex with SLX4CCD.”. X-ray diffraction, 2 ligands (ZN, CL), 1 pocket (best druggability 0.59). MolNFT v1 #110069 on GenesisL1: 3D structure, binding sites and…

PDB: 4XLG
Type: protein
Length: 327 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Structure-specific endonuclease subunit SLX4; Structure-specific endonuclease subunit SLX1
EC: 3.1.-.-
UniProt: Q6FJQ6, Q6FML9
Ligands: ZN, CL
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Structure-specific endonuclease subunit SLX4	protein	67	72% helix, 6% strand	Q6FJQ6
A	Structure-specific endonuclease subunit SLX1 (EC 3.1.-.-)	protein	260	42% helix, 18% strand	Q6FML9

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	217	0.59	0.80	38	empty

Interfaces

1 interface between chains.

B–A · 1178 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

4XLG · C. glabrata Slx1 in complex with Slx4CCD. · the same entry in another collection · chain B against B, TM-score 1.00
Q6FML9 · AlphaFold monomer V2.0 prediction for structure-specific endonuclease subunit SLX1… · a predicted model of the same protein · chain A against A, TM-score 0.98
Q6FJQ6 · AlphaFold monomer V2.0 prediction for structure-specific endonuclease subunit SLX4… · a predicted model of the same protein · chain B against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6FJQ6
Every structure of UniProt Q6FML9
Elsewhere: RCSB PDB 4XLG · PDBe 4XLG · UniProt Q6FJQ6 · UniProt Q6FML9

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