MolNFT v1 · #152796 · protein

The citrate-bound trimer of chemoreceptor MCP2201 ligand binding domain

6ITS · Methyl-accepting chemotaxis sensory transducer: “The citrate-bound trimer of chemoreceptor MCP2201 ligand binding domain”. X-ray diffraction, 3 pockets (best druggability 0.53). MolNFT v1 #152796 on GenesisL1: 3D structure, binding…

PDB: 6ITS
Type: protein
Length: 293 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl-accepting chemotaxis sensory transducer
UniProt: D0IVL9
Pockets: 3 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 88% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyl-accepting chemotaxis sensory transducer	protein	147	89% helix, 0% strand	D0IVL9
B	Methyl-accepting chemotaxis sensory transducer	protein	146	87% helix, 0% strand	D0IVL9

Ligands and binding sites

CIT · Citric acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.53	0.89	17	CIT
2	50	0.47	0.86	16	CIT
3	112	0.34	0.73	28	empty

Interfaces

1 interface between chains.

A–B · 172 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6ITS · The citrate-bound trimer of chemoreceptor MCP2201 ligand binding domain · 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 D0IVL9
Elsewhere: RCSB PDB 6ITS · PDBe 6ITS · UniProt D0IVL9

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