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Epidermal growth factor-like domain from human factor IX

Analyse Epidermal growth factor-like domain from human factor IX in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EDM
Type
protein
Length
78 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Factor IX
UniProt
P00740
Ligands
CA

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, CFactor IXprotein390% helix, 26% strandP00740

Ligands and binding sites

  • CA · Calcium ion · metal · 3 copies · chains B, C

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

Interfaces

1 interface between chains.

  • B–C · 398 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 1EDM · Epidermal growth factor-like domain from human factor IX · the same entry in another collection · chain C against C, TM-score 1.00
  • P00740 · AlphaFold monomer V2.0 prediction for coagulation factor IX (P00740) · a predicted model of the same protein · chain C against A, TM-score 0.93

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