MolNFT v1 · #5319 · protein

Crystal structure of mutm (fpg) protein from thermus thermophilus HB8

1EE8: “Crystal structure of mutm (fpg) protein from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.57). MolNFT v1 #5319 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1EE8
Type: protein
Length: 532 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mutm (fpg) protein
UniProt: O50606
Ligands: ZN
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Mutm (fpg) protein	protein	266	28% helix, 23% strand	O50606

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	255	0.57	0.78	33	empty
2	222	0.55	0.78	30	empty
3	197	0.48	0.75	29	empty

Interfaces

1 interface between chains.

A–B · 409 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1EE8 · Crystal structure of mutm (fpg) protein from thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
O50606 · AlphaFold monomer V2.0 prediction for formamidopyrimidine-DNA glycosylase (O50606) · 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 O50606
Elsewhere: RCSB PDB 1EE8 · PDBe 1EE8 · UniProt O50606

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