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Crystal structure of bovine beta-trypsin at 1.5 ångströms resolution in a crystal form with low molecular packing density. active site geometry, ion pairs and solvent structure

Analyse Crystal structure of bovine beta-trypsin at 1.5 ångströms resolution in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TLD
Type
protein
Length
223 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-trypsin
EC
3.4.21.4
UniProt
P00760
Ligands
CA, SO4

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-trypsin (EC 3.4.21.4)protein22310% helix, 36% strandP00760

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • SO4 · Sulfate ion · ion · chains A

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

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1TLD · Crystal structure of bovine beta-trypsin at 1.5 ångströms resolution in a crystal form… · the same entry in another collection · chain A against A, TM-score 1.00

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