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Unprocessed aspartate decarboxylase mutant, with alanine inserted at position 24

Analyse Unprocessed aspartate decarboxylase mutant, with alanine inserted at position 24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PYQ
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aspartate 1-decarboxylase
EC: 4.1.1.11
UniProt: P0A790
Ligands: SO4

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aspartate 1-decarboxylase (EC 4.1.1.11)	protein	120	14% helix, 48% strand	P0A790
B	Aspartate 1-decarboxylase (EC 4.1.1.11)	protein	116	15% helix, 48% strand	P0A790

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 983 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1PYQ · Unprocessed Aspartate Decarboxylase Mutant, with Alanine inserted at position 24 · the same entry in another collection · chain A against A, TM-score 1.00
P0A790 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (P0A790) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P0A790
Elsewhere: RCSB PDB 1PYQ · PDBe 1PYQ · UniProt P0A790

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