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Crystal structure of HFEN1 in apo form

Analyse Crystal structure of HFEN1 in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ZOD
Type: protein
Length: 260 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flap endonuclease 1
EC: 3.1.-.-
UniProt: P39748
Ligands: K, MG

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Flap endonuclease 1 (EC 3.1.-.-)	protein	260	48% helix, 12% strand	P39748

Ligands and binding sites

K · Potassium ion · metal · 4 copies · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

Compared structures

5ZOD · Crystal Structure of hFen1 in apo form · the same entry in another collection · chain A against A, TM-score 1.00
P39748 · AlphaFold monomer V2.0 prediction for flap endonuclease 1 (P39748) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P39748
Elsewhere: RCSB PDB 5ZOD · PDBe 5ZOD · UniProt P39748

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