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Crystal structure of a truncated variant of the human P73 tetramerization domain

Analyse Crystal structure of a truncated variant of the human P73 tetramerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WQJ
Type: protein
Length: 784 residues
Chains: 28
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P73
UniProt: O15350
Pockets: 11 · best druggability 0.86

Structure

x-ray diffraction · 11 distinct chains · 61% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tumor protein P73	protein	29	59% helix, 21% strand	O15350
B, L, 1	Tumor protein P73	protein	26	65% helix, 19% strand	O15350
C	Tumor protein P73	protein	32	66% helix, 22% strand	O15350
D, E, G, H, M, P, S, U, V, X	Tumor protein P73	protein	28	61% helix, 25% strand	O15350
F, Q	Tumor protein P73	protein	28	61% helix, 25% strand	O15350
I	Tumor protein P73	protein	29	66% helix, 24% strand	O15350
J, O, T, W, 2	Tumor protein P73	protein	27	63% helix, 26% strand	O15350
K	Tumor protein P73	protein	30	60% helix, 20% strand	O15350
N, R	Tumor protein P73	protein	29	59% helix, 24% strand	O15350
Y	Tumor protein P73	protein	26	54% helix, 27% strand	O15350
Z	Tumor protein P73	protein	31	55% helix, 23% strand	O15350

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	262	0.86	0.97	28	empty
2	226	0.85	0.97	28	empty
3	220	0.85	0.97	29	empty
4	212	0.84	0.97	28	empty
5	314	0.61	0.79	34	empty

Interfaces

91 interfaces between chains.

M–N · 1252 Å² buried · 24 hydrogen bonds · protein-protein
Q–R · 1249 Å² buried · 26 hydrogen bonds · protein-protein
S–T · 1193 Å² buried · 19 hydrogen bonds · protein-protein
C–D · 1189 Å² buried · 21 hydrogen bonds · protein-protein
I–J · 1186 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

2WQJ · Crystal structure of a truncated variant of the human p73 tetramerization domain · the same entry in another collection · chain G against G, 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 O15350
Elsewhere: RCSB PDB 2WQJ · PDBe 2WQJ · UniProt O15350

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