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Structure of the human P73 tetramerization domain (crystal form II)

Analyse Structure of the human P73 tetramerization domain (crystal form II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WTT
Type: protein
Length: 678 residues
Chains: 16
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P73
UniProt: O15350
Pockets: 9 · best druggability 0.75

Structure

x-ray diffraction · 12 distinct chains · 68% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Tumor protein P73	protein	42	69% helix, 17% strand	O15350
B	Tumor protein P73	protein	43	67% helix, 16% strand	O15350
C, K	Tumor protein P73	protein	42	71% helix, 17% strand	O15350
D	Tumor protein P73	protein	47	64% helix, 15% strand	O15350
F, N	Tumor protein P73	protein	42	74% helix, 14% strand	O15350
G	Tumor protein P73	protein	43	72% helix, 14% strand	O15350
H, J	Tumor protein P73	protein	45	67% helix, 13% strand	O15350
I	Tumor protein P73	protein	44	70% helix, 14% strand	O15350
L	Tumor protein P73	protein	46	65% helix, 15% strand	O15350
M	Tumor protein P73	protein	29	66% helix, 21% strand	O15350
O	Tumor protein P73	protein	41	59% helix, 10% strand	O15350
P	Tumor protein P73	protein	43	70% helix, 9% strand	O15350

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1048	0.75	0.78	76	empty
2	795	0.72	0.78	53	empty
3	574	0.62	0.74	54	empty
4	343	0.55	0.75	36	empty
5	85	0.40	0.78	16	empty

Interfaces

45 interfaces between chains.

I–J · 1213 Å² buried · 15 hydrogen bonds · protein-protein
C–D · 1209 Å² buried · 17 hydrogen bonds · protein-protein
E–F · 1208 Å² buried · 17 hydrogen bonds · protein-protein
K–L · 1168 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1150 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

2WTT · Structure of the human p73 tetramerization domain (crystal form II) · the same entry in another collection · chain A against A, 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 2WTT · PDBe 2WTT · UniProt O15350

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