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The atomic resolution crystal structure of kringle 2 variant bound with eaca

Analyse The atomic resolution crystal structure of kringle 2 variant bound with eaca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6DCM
Type
protein
Length
85 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Plasminogen
EC
3.4.21.7
Ligands
ACA

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APlasminogen (EC 3.4.21.7)protein857% helix, 18% strand—

Ligands and binding sites

  • ACA · 6-aminohexanoic acid · ligand · chains A

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

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 6DCM · The atomic resolution crystal structure of Kringle 2 variant bound with EACA · the same entry in another collection · chain A against A, TM-score 1.00

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