P64604: Intermembrane phospholipid transport system binding protein MlaD (mlaD)

Intermembrane phospholipid transport system binding protein MlaD (mlaD) is a 183-residue protein from Escherichia coli (strain K12). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P64604.

Gene
mlaD
Organism
Escherichia coli (strain K12)
Length
183 residues
Mean pLDDT
84.9
Model
AF-P64604-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 84.9 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate63%
70 to 90Confident: backbone generally right16%
50 to 70Low: treat with caution9%
Below 50Very low: often disordered regions12%

What pLDDT means and how to read it

Function

Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane (PubMed:19383799, PubMed:27529189). MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex (PubMed:27529189)

Subunit structure

The complex is composed of two ATP-binding proteins (MlaF), two transmembrane proteins (MlaE), two cytoplasmic solute-binding proteins (MlaB) and six periplasmic solute-binding proteins (MlaD) (PubMed:27529189, PubMed:28388411). Interacts with MlaC (PubMed:28388411)

Subcellular location

Cell inner membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5UW8X-ray2.15 ÅA/B/C/D/E/F/G=32-140
8HPZX-ray2.3 ÅA/B/C=29-183
8HQ9X-ray2.7 ÅA/B/C/D/E/F=29-183
5UW2X-ray2.85 ÅA/B/C=32-183
7CGEEM2.9 ÅG/H/I/J/K/L=1-183
8HQAX-ray3.2 ÅA/B/C=29-183
6ZY9EM3.3 ÅA/D/I/J/K/L=1-183
7CH0EM3.7 ÅG/H/I/J/K/L=1-183
7CGNEM4.3 ÅG/H/I/J/K/L=1-183
8OJ4EM4.35 ÅA/B/C/D/E/F=1-183
8OJGEM4.38 ÅA/B/C/D/E/F=1-183

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