MolNFT v1 · #165417 · protein

Human xpg, APO2 form

6TUS · DNA repair protein complementing xp-G CELLS,DNA repair…: “Human xpg, APO2 form”. X-ray diffraction, 1 ligand (SO4), 4 pockets (best druggability 0.50). MolNFT v1 #165417 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6TUS
Type: protein
Length: 583 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein complementing xp-G CELLS,DNA repair protein complementing xp-G cells
EC: 3.1.-.-
UniProt: P28715
Ligands: SO4
Pockets: 4 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair protein complementing xp-G CELLS,DNA repair protein complementing xp-G cells (EC 3.1.-.-)	protein	289	50% helix, 10% strand	P28715
B	DNA repair protein complementing xp-G CELLS,DNA repair protein complementing xp-G cells (EC 3.1.-.-)	protein	294	48% helix, 10% strand	P28715

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	225	0.50	0.75	31	empty
2	170	0.43	0.74	24	empty
3	88	0.38	0.76	21	empty
4	64	0.34	0.77	17	empty

Interfaces

1 interface between chains.

A–B · 681 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6TUS · human XPG, Apo2 form · the same entry in another collection · chain A against A, TM-score 1.00
P28715 · AlphaFold monomer V2.0 prediction for DNA repair protein complementing xp-G cells (P28715) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P28715
Elsewhere: RCSB PDB 6TUS · PDBe 6TUS · UniProt P28715

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