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Crystal structure of flap endonuclease-1 R42E mutant from pyrococcus horikoshii

Analyse Crystal structure of flap endonuclease-1 R42E mutant from pyrococcus horikoshii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MC8
Type: protein
Length: 662 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Flap endonuclease-1
UniProt: O50123
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Flap endonuclease-1	protein	331	38% helix, 8% strand	O50123

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	834	0.77	0.81	101	empty
2	136	0.75	0.94	27	empty
3	182	0.51	0.78	30	empty
4	178	0.49	0.77	25	empty
5	101	0.41	0.77	29	empty

Interfaces

1 interface between chains.

A–B · 817 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1MC8 · Crystal Structure of Flap Endonuclease-1 R42E mutant from Pyrococcus horikoshii · the same entry in another collection · chain A against A, TM-score 1.00
O50123 · AlphaFold monomer V2.0 prediction for flap endonuclease 1 (O50123) · a predicted model of the same protein · chain B against A, TM-score 0.89

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 O50123
Elsewhere: RCSB PDB 1MC8 · PDBe 1MC8 · UniProt O50123

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