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Crystal structure of the C2 domain of human coagulation factor V: complex with phenylmercury

Analyse Crystal structure of the C2 domain of human coagulation factor V: complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CZS
Type
protein
Length
160 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (coagulation factor V)
UniProt
P12259
Ligands
PHG

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (coagulation factor V)protein1604% helix, 49% strandP12259

Ligands and binding sites

  • PHG · Phenylmercury · ligand · chains A

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

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1CZS · Crystal structure of the C2 domain of human coagulation factor V: complex with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P12259 · AlphaFold monomer V2.0 prediction for coagulation factor V (P12259) · a predicted model of the same protein · chain A against A, TM-score 0.98

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