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Crystal structure of wild-type onconase at 1.65 a resolution

Analyse Crystal structure of wild-type onconase at 1.65 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3U00
Type: protein
Length: 104 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein P-30
EC: 3.1.27.-
UniProt: P22069
Ligands: PO4

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein P-30 (EC 3.1.27.-)	protein	104	19% helix, 40% strand	P22069

Ligands and binding sites

PO4 · Phosphate ion · ion · 5 copies · chains A

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

Modifications

Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).

Compared structures

3U00 · Crystal structure of wild-type onconase at 1.65 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
P22069 · AlphaFold monomer V2.0 prediction for protein P-30 (P22069) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P22069
Elsewhere: RCSB PDB 3U00 · PDBe 3U00 · UniProt P22069

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