GL1X · GenesisL1 explorer

Research workbench

Crystal structure of T.TH. HB8 L-aspartate-alpha-decarboxylase complexed with fumarate

Analyse Crystal structure of T.TH. HB8 L-aspartate-alpha-decarboxylase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2EEO
Type
protein
Length
118 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
Q5SKN7
Ligands
PYR, FUM

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAspartate 1-decarboxylase (EC 4.1.1.11)protein230% helix, 65% strandQ5SKN7
BAspartate 1-decarboxylase (EC 4.1.1.11)protein9519% helix, 44% strandQ5SKN7

Ligands and binding sites

  • PYR · Pyruvic acid · ligand · chains A, B
  • FUM · Fumaric acid · ligand · 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 · 1626 Ų buried · 27 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 2EEO · Crystal Structure of T.th. HB8 L-Aspartate-alpha-Decarboxylase Complexed with Fumarate · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5SKN7 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (Q5SKN7) · a predicted model of the same protein · chain B against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.