MolNFT v1 · #121205 · protein

P73 homo-tetramerization domain mutant I

5HOB · Tumor protein P73: “P73 homo-tetramerization domain mutant I”. X-ray diffraction, 1 ligand (MG), 3 pockets (best druggability 0.52). MolNFT v1 #121205 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5HOB
Type: protein
Length: 363 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P73
UniProt: O15350
Ligands: MG
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 8 distinct chains · 66% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tumor protein P73	protein	45	69% helix, 16% strand	O15350
B	Tumor protein P73	protein	45	62% helix, 16% strand	O15350
C	Tumor protein P73	protein	46	61% helix, 15% strand	O15350
D	Tumor protein P73	protein	43	72% helix, 16% strand	O15350
E	Tumor protein P73	protein	48	65% helix, 15% strand	O15350
F	Tumor protein P73	protein	44	68% helix, 16% strand	O15350
G	Tumor protein P73	protein	47	64% helix, 15% strand	O15350
H	Tumor protein P73	protein	45	67% helix, 16% strand	O15350

Ligands and binding sites

MG · Magnesium ion · metal · chains E, F

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	172	0.52	0.79	29	empty
2	98	0.43	0.78	25	empty
3	58	0.30	0.75	13	empty

Interfaces

17 interfaces between chains.

G–H · 1235 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 1180 Å² buried · 17 hydrogen bonds · protein-protein
C–D · 1153 Å² buried · 16 hydrogen bonds · protein-protein
E–F · 1141 Å² buried · 20 hydrogen bonds · protein-protein
E–G · 892 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5HOB · p73 homo-tetramerization domain mutant I · 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 5HOB · PDBe 5HOB · UniProt O15350

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