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Structure of alkaline phosphatase from the antarctic bacterium TAB5

Analyse Structure of alkaline phosphatase from the antarctic bacterium TAB5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2IUC
Type
protein
Length
682 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alkaline phosphatase
EC
3.1.3.1
UniProt
Q9KWY4
Ligands
MG, ZN, PO4

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlkaline phosphatase (EC 3.1.3.1)protein34034% helix, 24% strandQ9KWY4
BAlkaline phosphatase (EC 3.1.3.1)protein34233% helix, 24% strandQ9KWY4

Ligands and binding sites

  • MG · Magnesium ion · metal · 6 copies · chains A, B
  • ZN · Zinc ion · metal · 4 copies · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B
  • CAC · Cacodylate ion · additive · 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 · 1908 Ų buried · 26 hydrogen bonds · protein-protein

Compared structures

  • 2IUC · Structure of alkaline phosphatase from the Antarctic bacterium TAB5 · the same entry in another collection · chain A against A, TM-score 1.00

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