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The ligand binding domain of MLP24

Analyse The ligand binding domain of MLP24 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IOP
Type: protein
Length: 477 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl-accepting chemotaxis protein
UniProt: A0A0H6VSA0
Ligands: ALA, CA
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyl-accepting chemotaxis protein	protein	239	38% helix, 30% strand	A0A0H6VSA0
B	Methyl-accepting chemotaxis protein	protein	238	38% helix, 31% strand	A0A0H6VSA0

Ligands and binding sites

ALA · Alanine · ligand · chains B
CA · Calcium ion · metal · 2 copies · chains A, B
ACT · Acetate ion · 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	113	0.39	0.75	15	ACT

Interfaces

1 interface between chains.

A–B · 725 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

6IOP · The ligand binding domain of Mlp24 · 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 A0A0H6VSA0
Elsewhere: RCSB PDB 6IOP · PDBe 6IOP · UniProt A0A0H6VSA0

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