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Crystal structure of the TSG101-uev DOMAIN:SPACE group P21

Analyse Crystal structure of the TSG101-uev DOMAIN:SPACE group P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ZLX
Type: protein
Length: 1,721 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor susceptibility gene 101 protein
UniProt: Q99816
Ligands: SO4
Pockets: 20 · best druggability 0.63

Structure

x-ray diffraction · 9 distinct chains · 27% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tumor susceptibility gene 101 protein	protein	144	27% helix, 33% strand	Q99816
B	Tumor susceptibility gene 101 protein	protein	145	27% helix, 32% strand	Q99816
C, D	Tumor susceptibility gene 101 protein	protein	146	27% helix, 32% strand	Q99816
E	Tumor susceptibility gene 101 protein	protein	147	25% helix, 32% strand	Q99816
F, I	Tumor susceptibility gene 101 protein	protein	148	26% helix, 31% strand	Q99816
G, L	Tumor susceptibility gene 101 protein	protein	140	26% helix, 34% strand	Q99816
H	Tumor susceptibility gene 101 protein	protein	138	28% helix, 33% strand	Q99816
J	Tumor susceptibility gene 101 protein	protein	143	27% helix, 30% strand	Q99816
K	Tumor susceptibility gene 101 protein	protein	136	26% helix, 32% strand	Q99816

Ligands and binding sites

SO4 · Sulfate ion · ion · 10 copies · chains A, B, C, D, F, G, H, I, J, L

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	369	0.63	0.78	43	empty
2	351	0.60	0.77	31	empty
3	292	0.59	0.78	42	empty
4	511	0.59	0.73	45	empty
5	451	0.58	0.74	44	empty

Interfaces

13 interfaces between chains.

A–L · 628 Å² buried · 11 hydrogen bonds · protein-protein
C–E · 620 Å² buried · 9 hydrogen bonds · protein-protein
H–J · 601 Å² buried · 7 hydrogen bonds · protein-protein
G–I · 595 Å² buried · 8 hydrogen bonds · protein-protein
D–J · 565 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7ZLX · Crystal Structure of the TSG101-UEV domain:space group P21 · the same entry in another collection · chain L against L, TM-score 1.00

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 Q99816
Elsewhere: RCSB PDB 7ZLX · PDBe 7ZLX · UniProt Q99816

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