P47865: Aquaporin-1 (AQP1)

Aquaporin-1 (AQP1) is a 271-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47865.

Gene
AQP1
Organism
Bos taurus
Length
271 residues
Mean pLDDT
88.8
Model
AF-P47865-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 88.8 (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 accurate69%
70 to 90Confident: backbone generally right20%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions5%

What pLDDT means and how to read it

Function

Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues. Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol. In vitro, it shows non-selective gated cation channel activity and may be permeable to cations like K(+)…

Subunit structure

Homotetramer; each monomer provides an independent water pore (PubMed:11780053). Component of the ankyrin-1 complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 (By similarity). Interacts with EPHB2; involved in endolymph production in the inner ear (By similarity). Identified in a complex with STOM. Interacts (via the N-terminal) with ANK1 (via ANK 1-5…

Subcellular location

Cell membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
1J4NX-ray2.2 ÅA=1-271

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