MolNFT v1 · #95538 · protein

Crystal structure of amino acid residues 1-120 of CG17282

4IT6: “Crystal structure of amino acid residues 1-120 of CG17282”. X-ray diffraction, 1 pocket (best druggability 0.45). MolNFT v1 #95538 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4IT6
Type: protein
Length: 228 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CG17282
UniProt: Q9VDE4
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CG17282	protein	113	12% helix, 39% strand	Q9VDE4
B	CG17282	protein	115	14% helix, 39% strand	Q9VDE4

Ligands and binding sites

FMT · Formic acid · additive · 7 copies · chains A, B
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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	134	0.45	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 1894 Å² buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4IT6 · Crystal structure of amino acid residues 1-120 of CG17282 · 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 Q9VDE4
Elsewhere: RCSB PDB 4IT6 · PDBe 4IT6 · UniProt Q9VDE4

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