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Human carbonic anhydrase II in complex with (R)-1-aminopropan-2-ol

Analyse Human carbonic anhydrase II in complex with (R)-1-aminopropan-2-ol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SDJ
Type
protein
Length
258 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P00918
Ligands
BE7, J3K, HG, ZN

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein258—P00918

Ligands and binding sites

  • BE7 · (4-carboxyphenyl)(chloro)mercury · ligand · 2 copies · chains A
  • J3K · (2~{R})-1-azanylpropan-2-ol · ligand · chains A
  • HG · Mercury (II) ion · metal · 2 copies · chains A
  • ZN · Zinc ion · metal · chains A

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

Compared structures

  • 6SDJ · Human Carbonic Anhydrase II in complex with (R)-1-aminopropan-2-ol · the same entry in another collection · chain A against A, TM-score 1.00
  • P00918 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P00918) · a predicted model of the same protein · chain A against A, TM-score 0.99

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