P31644: Gamma-aminobutyric acid receptor subunit alpha-5 (GABRA5)

Gamma-aminobutyric acid receptor subunit alpha-5 (GABRA5) is a 462-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P31644.

Gene
GABRA5
Organism
Homo sapiens
Length
462 residues
Mean pLDDT
81.0
Model
AF-P31644-F1 v6
Model created
1 Aug 2025
PDB structures
23

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Model confidence (pLDDT)

The mean pLDDT of this model is 81.0 (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 accurate60%
70 to 90Confident: backbone generally right19%
50 to 70Low: treat with caution4%
Below 50Very low: often disordered regions18%

What pLDDT means and how to read it

Function

Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:14993607, PubMed:29961870, PubMed:30140029, PubMed:31056671). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:30140029). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:14993607, PubMed:30140029). GABAARs containing alpha-5/GABRA5 subunits are mainly…

Subunit structure

Heteropentamer, formed by a combination of alpha (GABRA1-6), beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho (GABRR1-3), pi (GABRP) and theta (GABRQ) chains, each subunit exhibiting distinct physiological and pharmacological properties

Subcellular location

Postsynaptic cell membrane, Cell membrane

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
8BHGX-ray2.39 ÅA/C/D/E=32-451
8BHBEM2.54 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
8BGIX-ray2.56 ÅA/B/C/D/E=32-346, A/B/C/D/E=424-450
8BHAEM2.67 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
8BHIEM2.67 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
8BHOEM2.93 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
8BHMEM2.95 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
9HNSEM3.1 ÅA/D=33-346, A/D=421-462
9RL5EM3.1 ÅA/D=23-346, A/D=421-462
9RPBEM3.1 ÅA/D=33-346, A/D=421-462
9HAAEM3.14 ÅA/D=33-346, A/D=421-462
9HNREM3.17 ÅA=33-346, A=421-462
5O8FX-ray3.2 ÅA/B/C/D/E=261-346, A/B/C/D/E=424-462
8BEJEM3.24 ÅA/B/C/D/E=32-345, A/B/C/D/E=424-450
8BHSEM3.24 ÅA/B/C/D/E=32-346, A/B/C/D/E=424-450
5OJMX-ray3.3 ÅA/B/C/D/E=261-346, A/B/C/D/E=424-462
8BHKEM3.3 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
8BHQEM3.3 ÅA/B/C/D/E=32-315, A/B/C/D/E=424-450
9HNTEM3.32 ÅA/D=33-346, A/D=421-462
9HUMEM3.35 ÅA/D=33-345, A/D=421-462

Showing 20 of 23 experimental structures (best resolution first).

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