MolNFT v1 · #115594 · protein

Crystal structure of uncharacterised protein Q1R1X2 from escherichia COLI UTI89

5COF · Uncharacterized protein: “Crystal structure of uncharacterised protein Q1R1X2 from escherichia COLI UTI89”. X-ray diffraction, 3 ligands (CA, NA, CL), 1 pocket (best druggability 0.42). MolNFT v1 #115594 on GenesisL1: 3D structure…

PDB: 5COF
Type: protein
Length: 172 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q1R1X2
Ligands: CA, NA, CL
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	172	62% helix, 5% strand	Q1R1X2

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.42	0.76	29	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

5COF · Crystal structure of Uncharacterised protein Q1R1X2 from Escherichia coli UTI89 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q1R1X2
Elsewhere: RCSB PDB 5COF · PDBe 5COF · UniProt Q1R1X2

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