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Enzymatic and structural characterisation of amphinase, a novel cytotoxic ribonuclease from rana pipiens oocytes

Analyse Enzymatic and structural characterisation of amphinase, a novel cytotoxic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2P7S
Type: protein
Length: 110 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amphinase-2
EC: 3.1.27.-
UniProt: P85073
Ligands: NAG

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amphinase-2 (EC 3.1.27.-)	protein	110	20% helix, 41% strand	P85073

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
ACT · Acetate ion · additive · 2 copies · chains A
GOL · Glycerol · additive · 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 glycan (disulfide, N-glycosylation).

Compared structures

2P7S · Enzymatic and Structural Characterisation of Amphinase, a Novel Cytotoxic Ribonuclease… · the same entry in another collection · chain A against A, TM-score 1.00
P85073 · AlphaFold monomer V2.0 prediction for amphinase-2 (P85073) · 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 P85073
Elsewhere: RCSB PDB 2P7S · PDBe 2P7S · UniProt P85073

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