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Crystal structure of escherichia COLI amine oxidase mutant E573Q

Analyse Crystal structure of escherichia COLI amine oxidase mutant E573Q in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EZZ
Type: protein
Length: 1,438 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P46883
Ligands: CU, CA

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	718	—	P46883
B	—	protein	720	—	P46883

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 9 copies · chains A, B

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

Compared structures

6EZZ · Crystal structure of Escherichia coli amine oxidase mutant E573Q · the same entry in another collection · chain A against A, TM-score 1.00
P46883 · AlphaFold monomer V2.0 prediction for primary amine oxidase (P46883) · a predicted model of the same protein · 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 P46883
Elsewhere: RCSB PDB 6EZZ · PDBe 6EZZ · UniProt P46883

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