MolNFT v1 · #53307 · protein

Crystal structure of the human P73 tetramerization domain

2WQI · Tumor protein P73: “Crystal structure of the human P73 tetramerization domain”. X-ray diffraction. MolNFT v1 #53307 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2WQI
Type: protein
Length: 177 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tumor protein P73
UniProt: O15350

Structure

x-ray diffraction · 4 distinct chains · 69% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tumor protein P73	protein	45	71% helix, 13% strand	O15350
B	Tumor protein P73	protein	43	74% helix, 14% strand	O15350
C	Tumor protein P73	protein	45	62% helix, 11% strand	O15350
D	Tumor protein P73	protein	44	68% helix, 11% strand	O15350

Interfaces

6 interfaces between chains.

A–B · 1122 Å² buried · 13 hydrogen bonds · protein-protein
C–D · 1092 Å² buried · 18 hydrogen bonds · protein-protein
B–D · 866 Å² buried · 10 hydrogen bonds · protein-protein
A–C · 864 Å² buried · 10 hydrogen bonds · protein-protein
A–D · 331 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2WQI · Crystal structure of the human p73 tetramerization domain · the same entry in another collection · chain C against C, TM-score 1.00
O15350 · AlphaFold monomer V2.0 prediction for tumor protein P73 (O15350) · a predicted model of the same protein · chain B against A, TM-score 0.76

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 2WQI · PDBe 2WQI · UniProt O15350

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