P0A407: Photosystem I P700 chlorophyll a apoprotein A2 (psaB)

Photosystem I P700 chlorophyll a apoprotein A2 (psaB) is a 741-residue protein from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1). This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P0A407.

Gene
psaB
Organism
Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Length
741 residues
Mean pLDDT
96.6
Model
AF-P0A407-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 96.6 (very high 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 accurate97%
70 to 90Confident: backbone generally right3%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6

Subunit structure

The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes

Subcellular location

Cellular thylakoid membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
7FIXEM1.97 ÅB1/B2/B3=1-741
1JB0X-ray2.5 ÅB=2-741
7M75X-ray2.75 ÅB=2-741
6TRAEM2.85 ÅB=1-741
6PFYX-ray2.9 ÅB/H/Z=1-741
6PGKX-ray2.9 ÅB/H/Z=1-741
6TRCEM2.98 Å2/B/b=1-741
7M76X-ray3.0 ÅB=2-741
7M78X-ray3.0 ÅB=2-741
6TRDEM3.16 Å2/B/b=1-741
6LU1EM3.2 ÅB=1-741
9LZJEM3.4 ÅaB/bB/cB=1-741
9LZKEM3.5 ÅB=1-741
1C51X-ray4.0 Å-
2PPSX-ray4.0 Å-
5ZF0X-ray4.2 ÅB1/B2/B3/B4/B5/B6=2-741
4FE1X-ray4.92 ÅB=2-741
7BW2X-ray6.5 ÅB=2-741
3PCQX-ray8.98 ÅB=2-741

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